ORIGINAL_ARTICLE
Comparative Assessment of the Whole-cell Pertussis Vaccine Potency Using Serological and Intracerebral Mouse Protection Methods
One of the most important QC tests of whole-cell pertussis vaccine (WCPV) is potency test. In this regard, mouse protection test (MPT) is the current potency method, which is associated with severe animal distress and large variability in results. The purpose of this study was to assess Pertussis Serological Potency Test (PSPT) as a serological alternative method to intracerebral challenge in MPT assay. In the current study, the potency of three experimental batches of WCPV (1, 2, and 3) and standard vaccine were compared using MPT and PSPT methods. In the MPT method, mice were immunized with tests and standard vaccines. After 2 weeks, they were intracerebrally challenged with Bordetella pertussis strain (18323). The potency was calculated via parallel line analysis based on the numbers of survivors 2 weeks after the challenge. Similar to MPT method, mice were immunized in the PSPT method and bled after 4 weeks. In the next step, sera were titrated by 18323-WCP-ELISA assay and potency values were estimated via parallel line analysis. Pearson correlation test was used to measure the strength of association between MPT and PSPT assay results. The potency values of the experimental laboratory batches 1, 2, and 3 in MPT assays were 11.14, 5.02, and 4.24 Iu/ml, whereas the obtained results of PSPT assays were 10.32, 4.11, and 3.06 Iu/ml, respectively. The correlation of MPT and PSPT results was 0.807. The findings of the present study demonstrated a significant correlation between MPT and PSPT results. The implementation of PSPT was more advantageous, compared to MPT due to its ethical approaches and less variability in results. The PSPT is a promising alternative method for intracerebral challenge. However, additional validation is needed to support the establishment of this method.
https://archrazi.areeo.ac.ir/article_118718_864359a70eb1dcd79ba1fcb4031cf7ea.pdf
2019-06-01
103
109
10.22092/ari.2018.108852.1096
MPT
PSPT
Potency
i.c. challenge
D.
Mohammadbagher
dm_1453@yahoo.com
1
Blood Transfusion Research Center, High Institute for Research and Education in Transfusion Medicine, Tehran, Iran
AUTHOR
M.
Noofeli
noofeli1234@yahoo.com
2
Department of Human Viral Vaccine Production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
LEAD_AUTHOR
G.
Karimi
g.karimi@ibto.ir
3
Blood Transfusion Research Center, High Institute for Research and Education in Transfusion Medicine, Tehran, Iran
AUTHOR
Black, RE., Cousens, S,, Johnson, HL., Lawn, JE., Rudan, I., Bassani, DG., 2010. Global, regional, and national causes of child mortality in 2008: a systematic analysis. The lancet. 375 (9730), 1969-87.
1
Chovel, ML., Mandiarote, A., Ontivero, I., Mahy, T., Herrera, L., Núñez, JF., 2012. Development of 3Rs alternatives for determining potency and toxicity of vaccines in Cuba: current challenges and research projects in progress. ALTEX 29, 71-6.
2
Corbel, MJ., Xing, DK., 2004. Toxicity and potency evaluation of pertussis vaccines. Expert review of vaccines. 3(1), 89-101.
3
Hoonakker, M., Verhagen, L., van der Maas, L., Metz, B., Uittenbogaard, J., van de Waterbeemd, B., 2016. Adaptive immune response to whole cell pertussis vaccine reflects vaccine quality: A possible complementation to the Pertussis Serological Potency test. Vaccine. 34 (37), 4429-36.
4
Kendrick, PL., Eldering, G., Dixon, MK., Misner, J., 1947. Mouse protection tests in the study of pertussis vaccine: a comparative series using the intracerebral route for challenge. American Journal of Public Health and the Nations Health. 37 (7), 803-10.
5
Matos, DCS., Marcovistz, R., Silva, AMVd., Quintilio, W., Georgini, RA., 2012. Comparative analysis of the intracerebral mouse protection test and serological methodfor potency assays of pertussis component in DTP vaccine. Brazilian Journal of Microbiology. 43 (2), 429-31.
6
Van der Ark, A., van Straaten-van de Kappelle, I., Akkermans, A., Hendriksen, C., van de Donk, H., 1994. Development of Pertussis Serological Potency Test: Serological assessment of antibody response induced by whole cell vaccine as an alternative to mouse protection in an intracerebral challenge model. Biologicals. 22 (3); 233-42.
7
Van der Ark, A., Van Straaten-van de Kappelle, I., Hendriksen, C., Van de Donk, H., 1995. Pertussis serological potency test as an alternatively to the intracerebral mouse protection test. Developments in biological standardization. 86, 271-81.
8
Van der Ark, A., van Straaten-van de Kappelle, I., Hendriksen, C., 1998.Pertussis serological potency test as an alternative to the intracerebral mouse protection test: development, evaluation and validation. ALTEX. 15 (5), 33-6.
9
Van der Ark, A., van Straaten-van de Kappelle, I., Ölander, R-M., Enssle, K., Jadhav, S., Van de Donk, H., 2000. The pertussis serological potency test collaborative study to evaluate replacement of the mouse protection test. Biologicals. 28 (2), 105-18.
10
Van Straaten, I., Levels, L., van der Ark, A., Thalen, M., Hendriksen, C., 2001. Toxicity and
11
Immunogenicity of pertussis whole cell vaccine in one animal model. Developments in
12
biologicals. 111, 47-55.
13
Von Hunolstein, C., Gomez Miguel, M., Pezzella, C., Scopetti, F., Behr-Gross, M., Halder, M., 2008. Evaluation of two serological methods for potency testing of whole cell pertussis vaccines. Pharmeuropa Bio 1, 7-18.
14
World Health Organization, WHO, 1990. Control of whole-cell pertussis vaccine, WHO Technical Report Series. No. 800, A.3.4. 133-138
15
World Health Organization, WHO, 2013. Manual for quality Control of Diphtheria, Tetanus and Pertussis vaccines. WHO/IVB/11.11. 175-190.
16
ORIGINAL_ARTICLE
Cloning and Expression of Mannheimia haemolytica PlpE Gene in Escherichia coli and its Immunogenicity Assessment
Mannheimia haemolytica is responsible for considerable economic losses to cattle, sheep, and goat industries in many parts of the world. This bacterium isone of the causative agents of shipping fever in cattle. Current vaccines against M. haemolytica are moderately efficacious since they do not provide complete protection against the disease. Production of an economic vaccine for protecting farm animals against M. haemolytica has attracted the attention of many scientists. The outer membrane proteins (OMPs) play a major role in the pathogenesis and immunogenicity of M. haemolytica. Research on M. haemolytica OMPs has shown that antibodies to a particular OMP may be important in immune protection. In the current study, the gene for M. haemolytica OMP PlpE was cloned into the expression vector pET26-b, and then expressed in Escherichia coli BL21. The expression of the protein was carried out by the induction of cultured Escherichiacoli Bl21 cells with 1mM isopropyl-β-D-thiogalactopyranoside. The recombinant PlpE was purified using Ni-NTA agarose resin, and then subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis. The identity of the expressed protein was analyzed by western blotting. It was revealed that rPlpE was expressed and produced properly. To assess the immunogenicity of the recombinant protein, the purified rPlpE was used as an antigen for antibody production in goats. The observations suggested that the produced recombinant protein can be used as a antigen for developing diagnostic tests and or as a vaccine candidate.
https://archrazi.areeo.ac.ir/article_118725_8c50d5a15c5e78aba5a2ef7fd2253edf.pdf
2019-06-01
111
118
10.22092/ari.2018.116479.1169
Mannheimia haemolytica
PlpE
Cloning
Expression
Immunogenicity
A.
Yektaseresht
azadeh_neisi@shirazu.ac.ir
1
Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
LEAD_AUTHOR
F.
Sabet Sarvestani
dfssarvestani@yahoo.com
2
Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
AUTHOR
M.
Dordani
mdordani.vet88@gmail.com
3
Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
AUTHOR
A.
Hosseini
arsalan.hosseini@gmail.com
4
Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
AUTHOR
Aubry, P., Warnick, L.D., Guard, C.L., Hill, B.W., Witt, M.F., 2001. Health and performance of young dairy calves vaccinated with a modified-live Mannheimia haemolytica and Pasteurella multocida vaccine. J Am Vet Med Assoc 219, 1739-1742.
1
Ayalew, S., Confer, A.W., Blackwood, E.R., 2004. Characterization of immunodominant and potentially protective epitopes of Mannheimia haemolytica serotype 1 outer membrane lipoprotein PlpE. Infect Immun 72, 7265-7274.
2
Ayalew, S., Confer, A.W., Payton, M.E., Garrels, K.D., Shrestha, B., Ingram, K.R., et al., 2008. Mannheimia haemolytica chimeric protein vaccine composed of the major surface-exposed epitope of outer membrane lipoprotein PlpE and the neutralizing epitope of leukotoxin. Vaccine 26, 4955-4961.
3
Belshe, R.B., Smith, M.H., Hall, C.B., Betts, R., Hay, A.J., 1988. Genetic basis of resistance to rimantadine emerging during treatment of influenza virus infection. J Virol 62, 1508-1512.
4
Confer, A.W., 1993. Immunogens of Pasteurella. Vet Microbiol 37, 353-368.
5
Confer, A.W., Ayalew, S., Panciera, R.J., Montelongo, M., Whitworth, L.C., Hammer, J.D., 2003. Immunogenicity of recombinant Mannheimia haemolytica serotype 1 outer membrane protein PlpE and augmentation of a commercial vaccine. Vaccine 21, 2821-2829.
6
Confer, A.W., McCraw, R.D., Durham, J.A., Morton, R.J., Panciera, R.J., 1995. Serum antibody responses of cattle to iron-regulated outer membrane proteins of Pasteurella haemolytica A1. Vet Immunol Immunop 47, 101-110.
7
Confer, A.W., Panciera, R.J., Fulton, R.W., Gentry, M.J., Rummage, J.A., 1985. Effect of vaccination with live or killed Pasteurella haemolytica on resistance to experimental bovine pneumonic pasteurellosis. Am J Vet Res 46, 342-347.
8
Confer, A.W., Panciera, R.J., Gentry, M.J., Fulton, R.W., 1987. Immunologic response to Pasteurella haemolytica and resistance against experimental bovine pneumonic pasteurellosis, induced by bacterins in oil adjuvants. Am J Vet Res 48, 163-168.
9
Conlon, J.A., Shewen, P.E., Lo, R.Y., 1991. Efficacy of recombinant leukotoxin in protection against pneumonic challenge with live Pasteurella haemolytica A1. Infect Immun 59, 587-591.
10
Eskandari, M.H., Hosseini. A., Alasvand Zarasvand, S., Aminlari, M., 2012. Cloning, Expression, Purification and Refolding of Caprine Prochymosin. Food Biotechnol 26, 143-53.
11
Gerlach, G.F., Anderson, C., Klashinsky, S., Rossi-Campos, A., Potter, A.A., Willson, P.J., 1993. Molecular characterization of a protective outer membrane lipoprotein (OmlA) from Actinobacillus pleuropneumoniae serotype 1. Infect Immun 61, 565-572.
12
Haag, A.F., Ostermeier, C., 2009. Positive-selection vector for direct protein expression. Biotechniques 46, 453-457.
13
Hodgson, J.C., Moon, G.M., Quirie, M., Donachie, W., 2003. Association of LPS chemotype of Mannheimia (Pasteurella) haemolytica A1 with disease virulence in a model of ovine pneumonic pasteurellosis. J Endotoxin Res 9, 25-32.
14
Morton, R.J., Panciera, R.J., Fulton, R.W., Frank, G.H., Ewing, S.A., Homer, J.T., et al., 1995. Vaccination of cattle with outer membrane protein-enriched fractions of Pasteurella haemolytica and resistance against experimental challenge exposure. Am J Vet Res 56, 875-879.
15
Mosier, D.A., Simons, K.R., Confer, A.W., Panciera, R.J., Clinkenbeard, K.D., 1989. Pasteurella haemolytica antigens associated with resistance to pneumonic pasteurellosis. Infect Immun 57, 711-716.
16
Pandher, K., Confer, A.W., Murphy, G.L., 1998. Genetic and immunologic analyses of PlpE, a lipoprotein important in complement-mediated killing of Pasteurella haemolytica serotype 1. Infect Immun 66, 5613-5619.
17
Pandher, K., Murphy, G.L., Confer, A.W., 1999. Identification of immunogenic, surface-exposed outer membrane proteins of Pasteurella haemolytica serotype 1. Vet Microbiol 65, 215-226.
18
Perino, L.J., Hunsaker, B.D., … 31, 1997. A review of bovine respiratory disease vaccine field efficacy. Bovine Pr 31, 59-66.
19
Potter, A.A., Schryvers, A.B., Ogunnariwo, J.A., Hutchins, W.A., Lo, R.Y., Watts, T., 1999. Protective capacity of the Pasteurella haemolytica transferrin-binding proteins TbpA and TbpB in cattle. Microb Pathog 27, 197-206.
20
Purdy, C.W., Livingston, C.W., Jr., Frank, G.H., Cummins, J.M., Cole, N.A., Loan, R.W., 1986. A live Pasteurella haemolytica vaccine efficacy trial. J Am Vet Med Assoc 188, 589-591.
21
Purdy, C.W., Raleigh, R.H., Collins, J.K., Watts, J.L., Straus, D.C., 1997. Serotyping and enzyme characterization of Pasteurella haemolytica and Pasteurella multocida isolates recovered from pneumonic lungs of stressed feeder calves. Curr Microbiol 34, 244-249.
22
Rahn, R., Thomaidis, G., Frenkel, G., Frank, P., Kinner, U., 1989. [Late results of conservative condylar fracture treatment]. Dtsch Z Mund Kiefer Gesichtschir 13, 197-202.
23
Rajeev, S., Kania, S.A., Nair, R.V., McPherson, J.T., Moore, R.N., Bemis, D.A., 2001. Bordetella bronchiseptica fimbrial protein-enhanced immunogenicity of a Mannheimia haemolytica leukotoxin fragment. Vaccine 19, 4842-4850.
24
Rice, J.A., Carrasco-Medina, L., Hodgins, D.C., Shewen, P.E., 2007. Mannheimia haemolytica and bovine respiratory disease. Anim Health Res Rev 8, 117-128.
25
Shewen, P.E., Wilkie, B.N., 1988. Vaccination of calves with leukotoxic culture supernatant from Pasteurella haemolytica. Can J Vet Res 52, 30-36.
26
Srinand, S., Hsuan, S.L., Yoo, H.S., Maheswaran, S.K., Ames, T.R., Werdin, R.E., 1996a. Comparative evaluation of antibodies induced by commercial Pasteurella haemolytica vaccines using solid phase immunoassays. Vet Microbiol 49, 181-195.
27
Srinand, S., Maheswaran, S.K., Ames, T.R., Werdin, R.E., Hsuan, S.-L., 1996b. Evaluation of efficacy of three commercial vaccines against experimental bovine pneumonic pasteurellosis. Vet Microbio 52, 81-89.
28
Studier, F.W., 2005. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41, 207-234.
29
Studier, F.W., Moffatt, B.A., 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189, 113-130.
30
Zecchinon, L., Fett, T., Desmecht, D., 2005. How Mannheimia haemolytica defeats host defence through a kiss of death mechanism. Vet Res 36, 133-156.
31
ORIGINAL_ARTICLE
Molecular Detection of Chlamydia felis in Cats in Ahvaz, Iran
Chlamydiae are obligate generally Gram-negative intracellular parasites with bacterial characteristics, including a cell wall, DNA, and RNA. They have a worldwide distribution in different animal species. Chlamydia felis (C. felis) is an important agent with zoonotic susceptibility often isolated from cats with chronic conjunctivitis. The aim of the present survey aimed to determine the molecular occurrence of C. felis in cats in Ahvaz, Iran. In this regard, a total of 152 cats (126 households and 26 feral) were included in the current study. After recording their history information, two swabs were taken from the oropharyngeal cavity and eye conjunctiva of the investigated cats. The extraction of DNA was followed by PCR targeting the pmp gene of C. Felis. In the next step, the positive samples were sequenced based on the Gene Bank. Out of 152 samples, 35 (23.03%) were positive using polymerase chain reaction technique (95% CI: 16.30-29.70). Regarding infection with Chlamydiosis, the obtained results showed a significant difference between cats suffering from ocular or respiratory diseases (44.64%; 25 out of 56) and the healthy ones (10.42%; 10 out of 96; P=0.01). The prevalence of infection was significantly higher in cats younger than 1 year (34.12%; 29 out of 85), compared to those older than 1 year (8.96%; 6 out of 67; P=0.02). No significant difference was noted in terms of gender (25.45% in males and 21.65% in females), breed (23.81% in DSH and 19.23% in Persian), and lifestyle (22.22% companions [28 out of 126] and 26.92% ferals [7 out of 26]; P>0.05). It can be concluded that a significant number of cats are infected with C. felis in Ahvaz. The use of molecular tests, such as PCR, has revolutionized the diagnosis of chlamydial infections.
https://archrazi.areeo.ac.ir/article_118726_85158c5e398b5a174dfdc0fcfeccd357.pdf
2019-06-01
119
126
10.22092/ari.2018.116617.1172
Chlamydia felis
Chlamydiosis
PCR
Ahvaz
Cat
M.
Barimani
barimani_babak@yahoo.com
1
Department of Clinical Sciences, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
AUTHOR
B.
Mosallanejad
bmosallanejad@scu.ac.ir
2
Department of Clinical Sciences, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
LEAD_AUTHOR
M.
Ghorbanpoor
m.ghorbanpoor@scu.ac.ir
3
Department of Clinical Sciences, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
AUTHOR
S.
Esmaeilzadeh
s_esmaeilzadeh@yahoo.com
4
Department of Clinical Sciences, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
AUTHOR
Bannasch, M.J., Foley, J.E., 2005. Epidemiologic evaluation of multiple respiratory pathogens in cats in animal shelters. J Feline Med Surg 7, 109-119.
1
Bommana, S., Pokinghorne, A., 2019. Mini Review: Antimicrobial control of chlamydial infections in Animals: Current practices and issues. Front Microbiol 10, 1-9.
2
Borel, N., Polkinghorne, A., Pospischil, A., 2018. A review on chlamydial diseases in animals: still a challenge for pathologists? Vet pathol 55, 374-390.
3
Cantekin, Z., Solmaz, H., Altug, N., Ozmen, G.O., 2014. Development of pmp Gene-Specific PCR Assay with A Host Specific Internal Control for Chlamydophila felis. Thai J Vet Med 44, 469.
4
Halánová, M., Sulinova, Z., Čisláková, L., Trbolova, A., Páleník, Ľ., Weissova, T., et al., 2011. Chlamydophila felis in Cats–Are the Stray Cats Dangerous Source of Infection? Zoonoses Public Hlth 58, 519-522.
5
Hartmann, A.D., Hawley, J., Werckenthin, C., Lappin, M.R., Hartmann, K., 2010. Detection of bacterial and viral organisms from the conjunctiva of cats with conjunctivitis and upper respiratory tract disease. J Feline Med Surg 12, 775-782.
6
Helps, C., Reeves, N., Egan, K., Howard, P., Harbour, D., 2003. Detection of Chlamydophila felis and feline herpesvirus by multiplex real-time PCR analysis. J Clin Microbiol 41, 2734-2736.
7
Johnson, F., 1984. Isolation of Chlamydia psittaci from nasal and conjunctival exudate of a domestic cat. Vet Rec 114, 342-344.
8
Kang, B.-T., Park, H.-M., 2008. Prevalence of feline herpesvirus 1, feline calicivirus and Chlamydophila felis in clinically normal cats at a Korean animal shelter. J Vet Sci 9, 207-209.
9
Maazi, N., Jamshidi, S., Kayhani, P., Momtaz, H., 2016. Occurrence of Chlamydophila felis, feline herpesvirus 1 and calcivirus in domestic cats of Iran. Iran J Microbiol 8, 312.
10
Masubuchi, K., Nosaka, H., Iwamoto, K., Kokubu, T., Yamanaka, M., Shimizu, Y., 2002. Experimental infection of cats with Chlamydophila felis. J Vet Med Sci 64, 1165-1168.
11
Millán, J., Rodríguez, A., 2009. A serological survey of common feline pathogens in free-living European wildcats (Felis silvestris) in central Spain. Eur J Wildlife Res 55, 285-291.
12
Momtaz, H., Alirezaie, M., Keyhani, P., 2014. Molecular detection of Chlamydophila felis in ocular discharge of domestic cats in Tehran & Isfahan. Biological Journal of Microorganism 3, 49-57.
13
Okuda, H., Ohya, K., Shiota, Y., Kato, H., Fukushi, H., 2011. Detection of Chlamydophila psittaci by using SYBR green real-time PCR. J Vet Med Sci 73, 249-254.
14
Rampazzo, A., Appino, S., Pregel, P., Tarducci, A., Zini, E., Biolatti, B., 2003. Prevalence of Chlamydophila felis and feline herpesvirus 1 in cats with conjunctivitis in northern Italy. J Vet Intern Med 17, 799-807.
15
Sandmeyer, L.S., Waldner, C.L., Bauer, B.S., Wen, X., Bienzle, D., 2010. Comparison of polymerase chain reaction tests for diagnosis of feline herpesvirus, Chlamydophila felis, and Mycoplasma spp. infection in cats with ocular disease in Canada. Canadian Vet J 51, 629-633.
16
Sibitz, C., Rudnay, E.C., Wabnegger, L., Spergser, J., Apfalter, P., Nell, B., 2011. Detection of Chlamydophila pneumoniae in cats with conjunctivitis. Vet Ophthalmol 14, 67-74.
17
Sykes, J.E., 2005. Feline chlamydiosis. Clin Tech Small An P 20, 129-134.
18
Sykes, J.E., Allen, J.L., Studdert, V.P., Browning, G.F., 2001. Detection of feline calicivirus, feline herpesvirus 1 and Chlamydia psittaci mucosal swabs by multiplex RT-PCR/PCR. Vet Microbiol 81, 95-108.
19
Sykes, J.E., Greene, C.E., 2012. Chlamydial infections. In: Greene, C.E. (Ed.), Infectious Diseases of the Dog and Cat, Missouri, St. Louis, pp. 270-276.
20
Wu, S.-M., Huang, S.-Y., Xu, M.-J., Zhou, D.-H., Song, H.Q., Zhu, X.-Q., 2013. Chlamydia felis exposure in companion dogs and cats in Lanzhou, China: a public health concern. BMC Vet Res 9, 104.
21
ORIGINAL_ARTICLE
A Case of Identity Confirmation of Brucella abortus S99 by Phage Typing and PCR Methods
Brucellosis is a zoonotic infection that is associated with fever in humans and abortion in animals. The agent of this disease is a facultative intracellular gram-negative coccobacillus called Brucella. There are six classic species, including B. abortus, B. melitensis, B. suis, B. canis, B. neotomae, and B. ovis. In recent years, four new species have been reported, including Brucella ceti, B. microti, B. pinnipedialis, and B. inopinata. Human disease causes hygienic and economic losses, including inactivity of workforces in the community and high cost of treatment. The disease also causes catastrophic losses in the livestock industry. There is no effective vaccine against human brucellosis. Hence, attempts to prevent human infection with Brucella are focused on preventative measures, including control of infection in livestock, which lead to a reduction in its incidence in humans. The common methods for diagnosis of this disease are serologic methods including Rose Bengal, Wright -2 ME and the ring test. B. abortus strain S99 is used to produce these diagnostic antigens. The production of these antigens requires the presence of a well-characterized seed with full identity. The aim of this work was confirmation of the identity of B. abortus S99 by phage typing, AMOS and multiplex PCR techniques. Therefore, it is essential to carry out the identification of the strains used as seed for the production of the brucellosis diagnostic antigens. In this project, B. abortus strain 99 was supplied by the bacterial collection of the Brucellosis Department of Razi Vaccine and Serum Research Institute. Then, the main aim of the present study was the confirmation of the seed identity by doing the tests through the standard phage typing method, AMOS PCR and multiplex PCR (Brucladder) methods. Results were in support of the identity of the studied strain, and the molecular methods could also be used as the sensitive approaches for validation of antigenic seed.
https://archrazi.areeo.ac.ir/article_118727_186029490d1fc57ecea6d99eea821d5d.pdf
2019-06-01
127
133
10.22092/ari.2019.123507.1255
Antigenic seed
Brucella abortus S99
Molecular test
Validation
S.
Alamian
s.alamian@rvsri.ac.ir
1
Department of Brucellosis, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
LEAD_AUTHOR
M.
Dadar
dadar.m77@gmail.com
2
Department of Brucellosis, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
S.
Soleimani
s.soleimani@rvsri.ac.ir
3
Department of Bio bank, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
A.M.
Behrozikhah
2112behroozikhah@gmail.com
4
Department of Brucellosis, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
A.
Etemadi
a.aetemady@yahoo.com
5
Department of Brucellosis, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran, Iran
AUTHOR
(FAO), F.a.A.O.o.t.U.N., 2010. Brucella melitensis in Eurasia and the Middle East. FAO Animal Production and Health Proceedings Rome.
1
(WHO), W.H.O., 2011. The control of neglected zoonotic diseases. In Report of the 3rd WHO Conference on the control of neglected zoonotic diseases: 'Community-based interventions for prevention and control of neglected zoonotic diseases'. WHO, Geneva.
2
Adone, R., Francia, M., Ciuchini, F., 2008. Brucella melitensis B115-based complement fixation test to detect antibodies induced by Brucella rough strains. J Appl Microbiol 105, 567-574.
3
Ahasan, M.S., Rahman, M.S., Rahman, A.K., Berkvens, D., 2017. Bovine and Caprine Brucellosis in Bangladesh: Bayesian evaluation of four serological tests, true prevalence, and associated risk factors in household animals. Trop Anim Health Prod 49, 1-11.
4
Alton, G., Jones, L., Angus, R., Verger, J., 1988a. Techniques for the Brucellosis laboratory, Paris.
5
Alton, G., Jones, L., Angus, R., Verger, J., 1988b. Techniques for the Brucellosis laboratory: Paris: Institute National de la Recherdie Agrononique.
6
Araj, G.F., 2010. Update on laboratory diagnosis of human brucellosis. Int J Antimicrob Agents 36, S12-S17.
7
Bounaadja, L., Albert, D., Chénais, B., Hénault, S., Zygmunt, M.S., Poliak, S., et al., 2009. Real-time PCR for identification of Brucella spp.: a comparative study of IS711, bcsp31 and per target genes. Vet Microbiol 137, 156-164.
8
Bricker, B.J., Halling, S.M., 1994. Differentiation of Brucella abortus bv. 1, 2, and 4, Brucella melitensis, Brucella ovis, and Brucella suis bv. 1 by PCR. J Clin Microbiol 32, 2660-2666.
9
Cunningham, B., Miler, J.J., Dolan, L., McKeon, F., O'Meara, M., 1980. Immunological characteristics in cattle of allergens derived from smooth Brucella abortus S99. Vet Rec 107, 369-375.
10
Ewalt, D.R., Bricker, B.J., 2000. Validation of the Abbreviated BrucellaAMOS PCR as a Rapid Screening Method for Differentiation ofBrucella abortus Field Strain Isolates and the Vaccine Strains, 19 and RB51. J Clin Microbiol 38, 3085-3086.
11
Getachew, T., Getachew, G., Sintayehu, G., Getenet, M., Fasil, A., 2016. Bayesian Estimation of Sensitivity and Specificity of Rose Bengal, Complement Fixation, and Indirect ELISA Tests for the Diagnosis of Bovine Brucellosis in Ethiopia. Vet Med Int 2016, 5.
12
Godfroid, J., Garin-Bastuji, B., Saegerman, C., Blasco, J., 2013. Brucellosis in terrestrial wildlife. Revue scientifique et technique-Office international des épizooties.
13
Goktas, P., Sumer, S., Oktay, G., Goktas, S., 1991. Bruselloz tanisindaiki test in karsilastirilmasi. Turk Microbiol Cem Derg 21, 199-203.
14
Gomez, M.C., Nieto, J.A., Rosa, C., Geijo, P., Escribano, M.A., Munoz, A., et al., 2008. Evaluation of seven tests for diagnosis of human brucellosis in an area where the disease is endemic. Clin Vaccine Immunol 15, 1031-1033.
15
Hanci, H., Igan, H., Uyanik, M.H., 2017. Evaluation of a new and rapid serologic test for detecting brucellosis: Brucella Coombs gel test. Pak J Biol Sci 20, 108-112.
16
Júnior, G.N., Megid, J., Mathias, L., Paulin, L., Vicente, A., Cortez, A., et al., 2017. Performance of microbiological, serological, molecular, and modified seminal plasma methods in the diagnosis of Brucella abortus in semen and serum of bovine bulls. Biologicals 48, 6-9.
17
López-Goñi, I., García-Yoldi, D., Marin, C., De Miguel, M., Munoz, P., Blasco, J., et al., 2008. Evaluation of a multiplex PCR assay (Bruce-ladder) for molecular typing of all Brucella species, including the vaccine strains. J Clin Microbiol 46, 3484-3487.
18
Manual, O., 2017. Bovine brucellosis. Manual of Diagnostic Tests and Vaccines for Terrestrial Animals, OIE, World Organisation for Animal Health.
19
Mert, A., Ozaras, R., Tabak, F., Bilir, M., Yilmaz, M., Kurt, C., et al., 2003. The sensitivity and specificity of Brucella agglutination tests. Diag Micr Infec Dis 46, 241-243.
20
Nielsen, K., 2002. Diagnosis of brucellosis by serology. Veterinary Microbiology 90, 447-459.
21
Reddy, A., Singh, D.K., Mantur, B.G., Kumar, A., Kumari, G., Rajagunalan, S., et al., 2014. Seroepidemiology of human brucellosis in Karnataka. J Vet Pub Hlth 12, 113-115.
22
Ruiz-Mesa, J., Sanchez-Gonzalez, J., Reguera, J., Martin, L., Lopez-Palmero, S., Colmenero, J., 2005. Rose Bengal test: diagnostic yield and use for the rapid diagnosis of human brucellosis in emergency departments in endemic areas. Clin Microbiol Infect 11, 221-225.
23
Song, L., Li, J., Hou, S., Li, X., Chen, S., 2012. Establishment of loop-mediated isothermal amplification (LAMP) for rapid detection of Brucella spp. and application to milk and blood samples. J Microbiol Meth 90, 292-297.
24
Wareth, G., Melzer, F., El‐Diasty, M., Schmoock, G., Elbauomy, E., Abdel‐Hamid, N., et al., 2017. Isolation of Brucella abortus from a Dog and a Cat confirms their Biological Role in Re‐emergence and Dissemination of Bovine Brucellosis on Dairy Farms. Transbound Emerg Dis 64, e27-e30.
25
Young, E.J., 1995. An overview of human brucellosis. Clin Infect Dis 21, 283-289.
26
Zowghi, E., Ebadi, A., Yarahmadi, M., 2008. Isolation and identification of Brucella organisms in Iran. Clin Infect Dis 3, 185-188.
27
ORIGINAL_ARTICLE
Molecular Characterization of a Three-disulfide Bridges Beta-like Neurotoxin from Androctonus crassicauda Scorpion Venom
Scorpion venom is the richest source of peptide toxins with high levels of specific interactions with different ion-channel membrane proteins. The present study involved the amplification and sequencing of a 310-bp cDNA fragment encoding a beta-like neurotoxin active on sodium ion-channel from the venom glands of scorpion Androctonus crassicauda belonging to the Buthidae family using reverse transcription polymerase chain reaction (RT-PCR) technique. The amplified complementary DNA (cDNA) fragment had a coding sequence of 240 bp. The deduced precursor open-reading frame was composed of 80 amino acid residues contain a signal peptide of 22 amino acid residues, followed by a mature toxin of 58 amino acids. It had a molecular mass of 6.84 kDa and isoelectric point of 4.58. The sequence similarity search revealed several matches with the scorpion toxin-like domain of toxin-3 superfamily with a homology range of 35- 75%. Multiple alignments and secondary structure prediction demonstrated that the toxin peptide deduced from the amplified cDNA was related to the long-chain neurotoxins in size but stabilized by three disulfide bridges instead of four. The level of difference implies that the corresponding genes have originated from a common ancestor. This level of difference may also confirm an evolutionary link between the ‘short-chain’ and ‘long-chain’ toxins. The analysis showed one major segment within this neurotoxin with maximal hydrophilicity which was predicted to be antigenic by inducing an antibody response.
https://archrazi.areeo.ac.ir/article_118717_21489510485b63d799c93294b9180910.pdf
2019-06-01
135
142
10.22092/ari.2018.105829.1028
Androctonus crassicauda
Beta-neurotoxin
Disulfide bridges
A.
Jolodar
jolodara@yahoo.com
1
Department of Basic Sciences, Biochemistry and Molecular Biology Section, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
LEAD_AUTHOR
Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J., 1990. Basic local alignment search tool. J MolBiol 215, 403-410.
1
Bougis, P.E., Rochat, H., Smith, L.A., 1989. Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II. J Biol Chem 264, 19259-19265.
2
Carbone, E., Wanke, E., Prestipino, G., Possani, L.D., Maelicke, A., 1982. Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin. Nature 296, 90-91.
3
DeBin, J.A., Maggio, J.E., Strichartz, G.R., 1993. Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am J Physiol 264, C361-369.
4
Farajzadeh-Sheikh, A., Jolodar, A., Ghaemmaghami, S., 2013. Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands. Iran Red Crescent Med J 15, 36-41.
5
Finn, R.D., Tate, J., Mistry, J., Coggill, P.C., Sammut, S.J., Hotz, H.R., et al., 2008. The Pfam protein families database. Nucleic Acids Res 36, D281-288.
6
Jouirou, B., Mouhat, S., Andreotti, N., De Waard, M., Sabatier, J.M., 2004. Toxin determinants required for interaction with voltage-gated K+ channels. Toxicon 43, 909-914.
7
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8
Kelley, L.A., Sternberg, M.J., 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4, 363-371.
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Kobayashi, Y., Takashima, H., Tamaoki, H., Kyogoku, Y., Lambert, P., Kuroda, H., et al., 1991. The cystine-stabilized alpha-helix: a common structural motif of ion-channel blocking neurotoxic peptides. Biopolymers 31, 1213-1220.
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Kolaskar, A.S., Tongaonkar, P.C., 1990. A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett 276, 172-174.
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Kopeyan, C., Martinez, G., Rochat, H., 1979. Amino acid sequence of neurotoxin III of the scorpion Androctonus austrialis Hector. Eur J Biochem 94, 609-615.
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Lebrun, B., Romi-Lebrun, R., Martin-Eauclaire, M.F., Yasuda, A., Ishiguro, M., Oyama, Y., et al., 1997. A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom. Biochem J 328 ( Pt 1), 321-327.
13
Loret, E.P., Mansuelle, P., Rochat, H., Granier, C., 1990. Neurotoxins active on insects: amino acid sequences, chemical modifications, and secondary structure estimation by circular dichroism of toxins from the scorpion Androctonus australis Hector. Biochemistry 29, 1492-1501.
14
Martin-Eauclaire, M.F., Ceard, B., Bosmans, F., Rosso, J.P., Tytgat, J., Bougis, P.E., 2005. New "Birtoxin analogs" from Androctonus australis venom. Biochem Biophys Res Commun 333, 524-530.
15
Nakagawa, Y., Lee, Y.M., Lehmberg, E., Herrmann, R., Herrmann, R., Moskowitz, H., et al., 1997. Anti-insect toxin 5 (AaIT5) from Androctonus australis. Eur J Biochem 246, 496-501.
16
Rochat, C., Sampieri, F., Rochat, H., Miranda, F., Lissitzky, S., 1972. Iodination of neurotoxins I and II of the scorpion Androctonus australis Hector. Biochimie 54, 445-449.
17
Srinivasan, K.N., Gopalakrishnakone, P., Tan, P.T., Chew, K.C., Cheng, B., Kini, R.M., et al., 2002. SCORPION, a molecular database of scorpion toxins. Toxicon 40, 23-31.
18
Thompson, J.D., Higgins, D.G., Gibson, T.J., 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680.
19
Valdivia, H.H., Possani, L.D., 1998. Peptide Toxins as Probes of Ryanodine Receptor Structure and Function. Trends CardiovasMed 8, 111-118.
20
von Heijne, G., 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14, 4683-4690.
21
Zeng, X.C., Corzo, G., Hahin, R., 2005. Scorpion venom peptides without disulfide bridges. IUBMB Life 57, 13-21.
22
Zeng, X.C., Luo, F., Li, W.X., 2006. Molecular dissection of venom from Chinese scorpion Mesobuthus martensii: identification and characterization of four novel disulfide-bridged venom peptides. Peptides 27, 1745-1754.
23
Zeng, X.C., Wang, S.X., Zhu, Y., Zhu, S.Y., Li, W.X., 2004. Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch. Peptides 25, 143-150.
24
Zhu, S., Gao, B., 2006. Molecular characterization of a new scorpion venom lipolysis activating peptide: Evidence for disulfide bridge-mediated functional switch of peptides. FEBS Lett 580, 6825-6836.
25
Zlotkin, E., Martinez, G., Rochat, H., Miranda, F., 1975. A protein toxic to crustacea from the venom of the scorpion Androctonus australis. Insect Biochemistry 5, 243-250.
26
Zlotkin, E., Rochat, H., Kopeyan, Miranda, F., Lissitzky, S., 1971. Purification and properties of the insect toxin from the venom of the scorpion Androctonus australis Hector. Biochimie 53, 1073-1078.
27
ORIGINAL_ARTICLE
Development of an Indirect Enzyme-linked Immunosorbent Assay to Detect Antibodies against Serotype A2013 of Foot and Mouth Disease Virus in Cattle
Foot and mouth disease (FMD) is a contagious animal disease that causes irreparable damage to the economy of countries, including Iran in which this disease is a native one. Among the ways to combat FMD are vaccination and slaughter. Due to the specific situation of Iran, it is not possible to kill infected animals. Therefore, vaccination is the most important way to fight this disease. Serum neutralization test (SNT) and enzyme-linked immunosorbent assay (ELISA) are two main methods to evaluate the safety and calculate antibody titer. In this study, an indirect ELISA test was developed based on the coating of a complete viral particle (140s) which made it possible to determine antibody. In addition, serotype and viral type were determined without the need for time-consuming and complex molecular tasks, including gene expression. Moreover, in case of a new epidemic, a new epidemic condition can be detected using a serum antibody method. However, the coating of the complete viral particle leads to virus purification as well as the conjugated anti-immunoglobulin antibody testing of the same animal. In this study, the SNT was used as a gold standard test to determine the serum antibody level and compare its results with indirect ELISA method to determine the sensitivity and specificity of the indirect ELISA. To measure the anti-virus antibody rate of FMD (type A2013) through receiver operating characteristic analysis with 100% sensitivity and the specificity of 90%, the routine formulas were utilized using 100 % and 82%sensitivity and specificity, respectively. In this study, the cutoff value for the optical density was obtained at 0.3 and there was a significant difference between the vaccinated animals and the unvaccinated ones in terms of antibody level against the A2013 type. This indicates the correctness of the test and the accurate and proportional antibody detection against the understudy viral types of FMD.
https://archrazi.areeo.ac.ir/article_118724_778616c520683ff5ef0c19e7f1f13b81.pdf
2019-06-01
143
155
10.22092/ari.2018.116378.1164
Antibody
Cattle
Cut off
Enzyme-linked immunosorbent assay
Foot and Mouth disease
Serum neutralization test
F.
Malekdar
r.malekdar@gmail.com
1
Department of Foot and Mouth Disease, Razi Vaccine and Serum Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
LEAD_AUTHOR
H.
Mahravani
h.mahravani@rvsri.ac.ir
2
Foot and Mouth Disease Reference Laboratory, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
A.
Sedigh
3
Department of Human Viral Vaccine, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
M.
Akbarzadegan
4
Foot and Mouth Disease Reference Laboratory, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
Abdollahi, D., Meshkat , M., 2004. Foot and Mouth Disease status in The Islamic Republic of Iran. Country report, Iran veterinary organization, p. Appendix 9.
1
Bachrach , H., Moore, D., McKercher, P., Polatnick, J., 1975. Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus. J Immunol.
2
Dagenais , P., Desprez, B., Alber, t., E, E., 1994. Direct Covalent Attachment of Small Peptide Antigens to Enzyme-Linked Immunosorbent Assay Plates Using Radiation and Carbodiimide Activation. Anal Biochem 222, Pages 149-155.
3
Emam, M., 1996. Studies on the effect of maternal immunity antibodies on the early aged vaccination with FMD vaccine. Ph. D. Thesis Faculty of Vetrinary Zagazig University, Infectious Diseases.
4
Fabrizio, C., Marradi, M., 2013. High Sensitive Detection of Carbohydrate Binding Proteins in an ELISA-Solid Phase Assay Based on Multivalent Glyconanoparticles. plos.
5
Hemmings, 2009. The importance of regular inlab checking of pipettes. Biohit. PDF http://www.fisher.co.uk/techzone/ pdfs/pipetting_techniques.pdf
6
Jamal, S., Belsham , G., 2013 Foot-and-mouth disease: past, present and future. Vet Res.
7
Jitendra, K.B., Sarita, J., Jajati, K., Moha, P., Punam, B., Bramhadev, P., 2013. Detection of antibodies specific for foot-and-mouth disease virus infection using indirect ELISA based on recombinant nonstructural protein 2B Arch Viral
8
Malekdar, F., Mahravani, H., 2017. Designing Indirect ELISA Test for Detection of Antibodies against Serotype A2013 & O2010 of Foot and Mouth Disease (FMD) Virus in Cattle. FMD department. Razi Vaccine and Serum Research Institute M.Sc., Karaj, pp. 45-120.
9
Mannonen, S., Nieminen, P., Kaasinen, J., Andersin, 2006. Raising the standard of mechanical pipetting. Biohit.PDF.
10
Mannonen, S., Tiusanen, T., Suovaniemi, O., 2000. Major sources of error of air displacement pipettors Biohit.PDF
11
Ming , Y., Tim , S., Satya, P., Kate, H., Lauro , V., Alfonso, C., et al., 2015. Development of a Competitive Enzyme-Linked Immunosorbent Assay for Detection of Antibodies against the 3B Protein of Foot-and-Mouth Disease Virus. Clin Vaccine Immunol.
12
Oh, J., Song, D., Yang , J., Song, J., Moon, H., Kim, T., et al., 2005. Comparison of an enzyme-linked immunosorbent assay with serum neutralization test for serodiagnosis of porcine epidemic diarrhea virus infection. J Vet Sci. , 349-352.
13
Oh, J.S., Song, D.S., Yang, J.S., 2005. Comparison of an enzyme-linked immunosorbent assay with serum neutralization test Veterinary Science, 349–352.
14
Schultheiss, O.C., Stanton, S.J., Jones, E., Beer, J.S., 2009. Assessment of salivary hormones. Methods in Social Neuroscience New York: Guilford Press.
15
Shojaee, M., Zibaei, S., January 2017. Purification of 146s Antigen of Foot-and-Mouth Disease (FMD) Virus Serotypes Aby Using the Sucrose Gradient Procedure. Int J Infect.
16
Tekleghiorghis, T., Weerdmeester , k., 2014. Comparison of Test Methodologies for Foot-and-Mouth Disease Virus Serotype A Vaccine Matching.Clin Vaccine Immunol, 674–683.
17
Yang , M., Parida , S., Salo, T., Hole, K., Velazquez-Salinas, L., Clavijo , A., 2015. Development of a Competitive Enzyme-Linked Immunosorbent Assay for Detection of Antibodies against the 3B Protein of Foot-and-Mouth Disease Virus. Clin Vaccine Immunol., 389-397.
18
ORIGINAL_ARTICLE
Comparison of Relation between Resistance Pattern to Erythromycin and Tetracycline and the Prevalence of Superantigens Coding Enterotoxins A and B in Staphylococcus aureus Isolated from Broiler Poultry in Ilam, Iran
Staphylococcus aureus is a gram-positive coccus that, in specific conditions, is able to generate various diseases. By secreting different enterotoxins, this bacterium prepares the settings to attack the host; among these, enterotoxins A and B play the most important roles in food poisoning. This study was performed to trace the genes coding enterotoxins A and B in Staphylococcus aureus isolated from the clinic and poultry slaughterhouse. In addition, the present study analyzed the relation between the prevalence of these genes and resistance to erythromycin and tetracycline. This study was performed from October 2015 to December 2016. A total of 200 samples of noses and cloaca from broiler poultry farms in Ilam, Iran, were collected, including 150 samples from the slaughterhouse and 50 samples from the clinic isolated for separating Staphylococcus aureus. After bacterial culture and confirmation of biochemical tests, the samples were evaluated for the identification of Staphylococcus aureus and the resistance pattern to antibiotics regarding the presence of femA, tets, ermb, sea, and seb genes using the disk diffusion method and polymerase chain reaction test. Out of 200 tested samples, 112 strains of Staphylococcus aureus (56%) were identified from which 91 and 21 strains were associated with the poultry slaughterhouse and clinic, respectively, and all the samples were identified using biochemical tests. After the detection of femA gene as an exclusive gene for the identification of Staphylococcus aureus strain, 100 strains (50%) were confirmed to be contaminated with this bacterium. Out of 100 strains, 46%, 14%, and 5% possessed the genes coding enterotoxin A, the genes coding enterotoxin B, and both genes, respectively. The results of antibiotic tests showed that 85% and 86% of the examined strains were resistant to erythromycin and tetracycline, respectively. In the present study, the analysis performed using QuickCalcs software showed that the strains resistant to these two antibiotics possessing the sea gene were more prevalent than those possessing seb genes in the samples isolated from the poultry slaughterhouse. This comparison revealed that during the short period of broiler poultry farms growth, resistant strains were able to proliferate sea gene among the herd, and its prevalence increased until reaching into the slaughterhouse. This study showed that the relation between the genes resistant to erythromycin and tetracycline and the sea gene was close and significant.
https://archrazi.areeo.ac.ir/article_118723_b32825c62905fee2d59422f226384f26.pdf
2019-06-01
157
164
10.22092/ari.2018.116231.1161
Staphylococcus aureus
Poultry
Enterotoxins A & B
L.
Mojahed Asl
lila.mojahed@yahoo.com
1
Department of Microbiology, School of Para Veterinary Medicine, Ilam University, Ilam, Iran
AUTHOR
K.
Saleki
kmzm97@gmail.com
2
Department of Microbiology, School of Para Veterinary Medicine, Ilam University, Ilam, Iran
LEAD_AUTHOR
M.
Nemati
m.nemati@ilam.ac.ir
3
Department of Microbiology, School of Para Veterinary Medicine, Ilam University, Ilam, Iran
AUTHOR
Alibayov, B., Zdeňková, K., Purkrtová, S., Demnerová, K., Karpíšková, R., 2014. Detection of some phenotypic and genotypic characteristics of staphylococcus aureus isolated from food items in the Czech Republic. Ann Microbiol 64, 1587-1596.
1
Barati, B., Saadati, M., Bahmani, M.K., 2006. Isolation and Detection of Enterotoxigenic Staphylococcus aureus type A by multiplex PCR. J Military Med 8, 28-119.
2
Bergdoll, M., 1983. Enterotoxins. Staphylococci and Staphylococcal infections, Academic Press, London.
3
Bystron, J., Molenda, J., Bania, J., Kosek-Paszkowska, K., Czerw, M., 2005. Occurrence of enterotoxigenic strains of Staphylococcus aureus in raw poultry meat. Pol J Vet Sci 8, 37-40.
4
Casman, E.P., Bennett, R.W., Dorsey, A.E., Issa, J.A., 1967. Identification of a fourth staphylococcal enterotoxin, enterotoxin D. J Bacteriol 94, 1875-1882.
5
Chiang, Y.C., Liao, W.W., Fan, C.M., Pai, W.Y., Chiou, C.S., Tsen, H.Y., 2008. PCR detection of Staphylococcal enterotoxins (SEs) N, O, P, Q, R, U, and survey of SE types in Staphylococcus aureus isolates from food-poisoning cases in Taiwan. Int J Food Microbiol 121, 66-73.
6
Cui, J.C., Zhang, B.J., Lin, Y.C., Wang, Q.K., Qian, A.D., Nakane, A., et al., 2010. Protective effect of glutathione S-transferase-fused mutant staphylococcal enterotoxin C against Staphylococcus aureus-induced bovine mastitis. Vet Immunol Immunopathol 135, 64-70.
7
Eshraghi, S., Salehipour, Z., Pourmand, M., Rahimi, F.A., Zahraei, S.M.T., Agha, A.S., et al., 2009. Prevalence of tst, entC, entA and entA/C genes in staphylococcus aureus strains isolated from different foods.
8
Feizi, A., Nazeri, M., Pilevar, A., 2012. Isolation of Staphylococcus spp. genera from broiler breeder flocks in East Azerbaijan Province of Iran: Prevalence and antimicrobial susceptibility.
9
Ifesan, B.O., Voravuthikunchai, S.P., 2009. Effect of Eleutherine americana Merr. extract on enzymatic activity and enterotoxin production of Staphylococcus aureus in broth and cooked pork. Foodborne Pathog Dis 6, 699-704.
10
Imani-Fooladi, A., Riazipour, M., Sattari, M., 2009. Comparison of molecular and serologic identification of Staphylococcus producing enterotoxins from dairy products traditionally. J Shahrekord U Med Sci 11th period 4, 19-26.
11
Khakpoor, M., Ezzati, M., Mahmoodi, K., Khalaji Pirbaluti, M., Khaksar, R., 2013. Prevalence of Coagulase-positive Staphylococcus aureus in local Cheese in West Azerbaijan with culture and PCR method. Iranian Journal of Nutrition Sciences & Food Technology 7, 238-242.
12
Lim, S.K., Joo, Y.S., Moon, J., Lee, A.R., Nam, H.M., Wee, S.H., et al., 2004. Molecular typing of enterotoxigenic Staphylococcus aureus isolated from bovine mastitis in Korea. J Vet Med Sci 66, 581-584.
13
Mashouf, R.Y., Hosseini, S.M., Mousavi, S.M., Arabestani, M.R., 2015. Prevalence of Enterotoxin Genes and Antibacterial Susceptibility Pattern of Staphylococcus aureus Strains Isolated from Animal Originated Foods in West of Iran. Oman Med J 30, 283-290.
14
Parsaeimehr, M., Basti, A.A., Radmehr, B., Misaghi, A., Abbasifar, A., KarimG., et al., 2010. Effect of Zataria multiflora Boiss. essential oil, nisin, and their combination on the production of enterotoxin C and alpha-hemolysin by Staphylococcus aureus. Foodborne Pathog Dis 7, 299-305.
15
Reischl, U., Linde, H.J., Metz, M., Leppmeier, B., Lehn, N.,2000. Rapid identification of methicillin-resistant Staphylococcus aureus and simultaneous species confirmation using real-time fluorescence PCR. J Clin Microbiol 38, 2429-2433.
16
Rodriguez, M., Nunez, F., Cordoba, J.J., Bermudez, E.,
17
Asensio, M.A., 1996. Gram-positive, catalase-positive cocci from dry cured Iberian ham and their enterotoxigenic potential. Appl Environ Microbiol 62, 1897-1902.
18
Saadati, M., Barati, B., Doroudian, M., Shirzad, H., Hashemi, M., Hosseini, S.M., et al., 2008. Detection of sea, sec and seq genes in Staphylococcus aureus nasal sampling acquiring from healthy carriers in Tehran province, Iran; by multiplex PCR. J Paramed Sci 2, 34-40.
19
Salari-Sharif, A., Sattari, M., Moradi, M., Shahrokhabadi, R., 2012. Detecting enterotoxin A and B genes of Staphylococcus bacteria in samples of clinical patients visiting treatment sources of Kerman and Rafsanjan using the molecular method. J Rafsanjan U Med Sci 11, 128-136.
20
Shapury, R., Rahnema, M., Eghbal Zadeh, S., 2009. The Prevalence of Salmonella serotypes in poultry and eggs, and determine antibiotic susceptibility of them in the Zanajan city. Q J Anim Phisiol Dev 3, 63-71.
21
Shekarforoush, S.S., Kiaie, S.M.M., Karim, G., Razavi Rohani, S.M., Rokni, N., Abbasvali, M., 2013. Study on the overview on foodborne bacteria in food with animal origin in Iran; Part four: Poultry and egg. J Food Hyg 3, 45-64.
22
Wang, S.-J., Chow, L.-W., Wu, M.-J., 2002. Multiplex PCR for the simultaneous detection of the SEA, SEB, SEC, SED and SEE genes of enterotoxigenic staphylococcus aureus.
23
ORIGINAL_ARTICLE
Cytomegalovirus Seroepidemiology: a Population-based Study in Alborz Province, Iran
Cytomegalovirus (CMV) is a type of herpes virus. This virus is one of the most common causes of congenital and prenatal infections. CMV infection in pregnant women, especially in the first trimester, may lead to congenital abnormalities in newborns. The prevalence of CMV infection in developed countries is approximately 40%, and in developing countries, this prevalence may be up to 100%. Because there is no information available related to the seroepidemiological patterns of this infection in different cities of Alborz province, Iran, this study was conducted. This seroprevalence study was based on sera collected from adults who were referred to health care providers or Medical Diagnostic Laboratory Centers (MDLS) in Alborz province, Iran, from 2011 to 2015 for different purposes. Using ELISA (IgG), a retrospective serological survey of CMV antibodies in serum samples was performed in a non-immunized community. Frozen sera from 2001 individuals who were randomly selected by a cluster sampling technique were collected from spring 2013 to winter 2015. Seroprevalence was stratified by age (>1 to <50 years). Mathematical techniques were used to determine whether there is a relationship between CMV seroprevalence and age, sex, and level of education in this community. Data were analyzed using Fisher’s exact test and the χ2 test using SPSS software version 11.5. The mean age of seropositive individuals varied between 15 and 50 years. CMV IgG was found in 1813 (91%) of 2001 individuals. In total, 188 individuals (9%) were negative for CMV IgG. There were significant relationships between seropositivity (CMV IgG) and age, sex, level of education, and level of antibody titer by sex. As in other developing countries, the prevalence of CMV infection in adults in Alborz province is high. Since CMV infection is prevalent and there are potential abnormalities associated with it, we strongly recommend the expansion of preventive measures and the establishment of programs to inform at-risk populations, especially vulnerable populations such as transplant recipients, immunocompromised patients, and school children on how to prevent this infection and its associated consequences.
https://archrazi.areeo.ac.ir/article_118728_8a2998b3a73b62fd9bcc54620afe5ecc.pdf
2019-06-01
165
173
10.22092/ari.2018.115919.1157
Cytomegalovirus
ELISA
Alborz
Iran
A.
Mohammadi
amohammadi43@gmail.com
1
Department of Human Viral Vaccine Production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
LEAD_AUTHOR
B.
Karbasi
b_karbasi2011@yahoo.com
2
Department of Bacteriology, Faculty of Medicine, Rasht Azad University, Rasht, Iran
AUTHOR
R.
Shahbazi
r.shahbazi@rvsri.ac.ir
3
Department of Human Viral Vaccine Production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
A.
Foroughi
a.foroughi@rvsri.ac.ir
4
Department of Human Viral Vaccine Production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
L.
Mokhber-alsafa
l.mokhber-alsafa@rvsri.ac.ir
5
Department of Health, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
Aarnisalo, J., Ilonen, J., Vainionpaa, R., Volanen, I., Kaitosaari, T., Simell, O., 2003. Development of antibodies against cytomegalovirus, varicella-zoster virus and herpes simplex virus in Finland during the first eight years of life: a prospective study. Scand J Infect Dis 35, 750-753.
1
Abuharfeil, N., Meqdam, M.M., 2000. Seroepidemiologic study of herpes simplex virus type 2 and cytomegalovirus among young adults in northern Jordan. New Microbiol 23, 235-239.
2
de Mattia, D., Stroffolini, T., Arista, S., Pistoia, D., Giammanco, A., Maggio, M., et al., 1991. Prevalence of cytomegalovirus infection in Italy. Epidemiol Infect 107, 421-427.
3
de Ory, F., Ramirez, R., Garcia Comas, L., Leon, P., Sagues, M.J., Sanz, J.C., 2004. Is there a change in cytomegalovirus seroepidemiology in Spain? Eur J Epidemiol 19, 85-89.
4
Dolar, N., Serdaroglu, S., Yilmaz, G., Ergin, S., 2006. Seroprevalence of herpes simplex virus type 1 and type 2 in Turkey. J Eur Acad Dermatol Venereol 20, 1232-1236.
5
Dowd, J.B., Haan, M.N., Blythe, L., Moore, K., Aiello, A.E., 2008. Socioeconomic gradients in immune response to latent infection. Am J Epidemiol 167, 112-120.
6
Ghazi, H.O., Telmesani, A.M., Mahomed, M.F., 2002. TORCH agents in pregnant Saudi women. Med Princ Pract 11, 180-182.
7
Glaser, R., 2005. Stress-associated immune dysregulation and its importance for human health: a personal history of psychoneuroimmunology. Brain Behav Immun 19, 3-11.
8
Kothair, A., Ramachandran, V.G., Gupta, P., Singh, B., Talwar, V., 2002. Seroprevalance of cytomegalovirus among voluntary blood donors in Delhi, India. J Health Popul Nutr 20, 348-351.
9
Mocarski, E.S., Shenk, T., Griffiths, P.D., Pass, R.F., 2013. Cytomegalovirus. In: Knipe, D.M., Howley, P.M. (Eds.), Field's Virology, Lippincott Williams & Wilkins, Philadelphia, pp. 1960-2014.
10
Smith, J.S., Robinson, N.J., 2002. Age-specific prevalence of infection with herpes simplex virus types 2 and 1: a global review. J Infect Dis 186 Suppl 1, S3-28.
11
Staras, S.A., Flanders, W.D., Dollard, S.C., Pass, R.F., McGowan, J.E., Jr., Cannon, M.J., 2008. Influence of sexual activity on cytomegalovirus seroprevalence in the United States, 1988-1994. Sex Transm Dis 35, 472-479.
12
Stroffolini, T., Ngatchu, T., Chiaramont, M., Giammanco, A., Maggio, M., Sarzana, A., et al., 1993. Prevalence of cytomegalovirus seropositivity in an urban childhood population in Cameroon. New microbial 16, 5-83.
13
Suassuna, J., Lopes Leite, L., Helena Cavalheiro Villela, L., 1995. Prevalence of cytomegalovirus infection in different patient groups of an urban University in Brazil.
14
ORIGINAL_ARTICLE
Effect of Gamma Irradiation on Microbial Decontamination, Crude Nutrient Content, and Mineral Nutrient Composition of Laboratory Animal Diets
Laboratory animal models are an important part of test design. Certain conditions such as microbial contamination in diets of these models could affect the results of experiments. One of the most important routes that predispose to contamination is generated through feeding of laboratory animals. This study aimed to show the effect of gamma irradiation in reducing bacteria concentrations, crude nutrient content, and concentrations of some minerals and trace elements in laboratory animal diets. Large-sized pellets with 10–15 mm diameter (commonly used for rats and hamsters) and small-sized pellets with 3–5 mm diameter (used for rabbits and guinea pigs) along with skimmed milk powder (SMP) as a food additive were exposed to gamma irradiation with different doses ranging from 3 to 30 kGy. The total microbial contamination and any possible changes in some mineral nutrient composition and the crude nutrient content were determined pre- and post-irradiation. Our data revealed that 25 kGy in pelleted diets and 18 kGy in SKM had superior effects in the reduction of bacterial contamination with little change in crude nutrient content and minerals and trace elements in nutrient requirements of laboratory animals. According to the results, gamma irradiation had minimal effects on crude nutrient content and the concentrations of some minerals and trace elements of laboratory animal diets, and it also eliminated bacterial and fungal contamination load. By using gamma irradiation, this method could yield a favorable outcome in controlling microbial contamination of animal diets.
https://archrazi.areeo.ac.ir/article_118722_0770490f39766a063f2f522a692b1a7e.pdf
2019-06-01
175
182
10.22092/ari.2017.116153.1160
Gamma Irradiation
Laboratory animal
Diet
Bacteria
Pellet
G.
Shahhosseini
gshahhosseini@yahoo.com
1
Nuclear Agriculture Research School, Nuclear Science and Technology Research Institute, Karaj, Iran
AUTHOR
A.
Karimi
karimia@tbzmed.ac.ir
2
Department of Molecular Medicine, Faculty of Advanced Medical Sciences, Tabriz University of Medical Sciences, Tabriz, Iran
LEAD_AUTHOR
S.
Amanpour
saeidamanpour@yahoo.com
3
Cancer Biology Research Center, Tehran University of Medical Sciences, Tehran, Iran
AUTHOR
M.A.
Mansouri
mansouri1339@yahoo.com
4
Department of Research, Breeding and Production of Laboratory Animals, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
(APHIS), 2017. U.S. Department of Agriculture's Animal and Plant Health Inspection Service Annual Report Animal Usage by Fiscal Year.
1
Adamiker, D., 1975. A comparison of various methods for treating feedstuffs for laboratory animals. Food Irrad Info 5, 19-42.
2
Adamiker, D., 1976. Irradiation of laboratory animal diets. A review. Z Versuchstierkd 18, 191-201.
3
Al-Masri, M.R., Zarkawi, M., 1994. Effects of gamma irradiation on chemical compositions of some agricultural residues. Radiat Phys Chem 43, 257-260.
4
Analytical-Methods-Committee, 2000. Determination of thiamine and riboflavin in pet foods and animal feedingstuffs. Analyst 125, 353-360.
5
Arvanitoyannis, I.S., Stratakos, A.C., 2010. Potential Uses of Irradiation. Irradiation of Food Commodities, Academic Press, Boston, pp. 635-669.
6
Caulfield, C.D., Cassidy, J.P., Kelly, J.P., 2008. Effects of gamma irradiation and pasteurization on the nutritive composition of commercially available animal diets. J Am Assoc Lab Anim Sci 47, 61-66.
7
Chiang, Y.-C., Huang, G.-J., Ho, Y.-L., Hsieh, P.-C., Chung, H.-P., Chou, F.-I., et al., 2010. Influence of gamma irradiation on microbial load and antioxidative characteristics of Polygoni Multiflori Radix. Process Biochem 46, 777-782.
8
Clarke, H.E., Coates, M.E., Eva, J.K., Ford, D.J., Milner, C.K., O'Donoghue, P.N., et al., 1977. Dietary standards for laboratory animals: report of the Laboratory Animals Centre Diets Advisory Committee. Lab Anim 11, 1-28.
9
Cowie, R.A., Makkar, H.P., 2013. Quality assurance for microbiology in feed analysis laboratories, FAO.
10
DeRouchey, J.M., Tokach, M.D., Nelssen, J.L., Goodband, R.D., Dritz, S.S., Woodworth, J.C., et al., 2003. Effect of irradiation of individual feed ingredients and the complete diet on nursery pig performance. J Anim Sci 81, 1799-1805.
11
DeRouchey, J.M., Tokach, M.D., Nelssen, J.L., Goodband, R.D., Dritz, S.S., Woodworth, J.C., et al., 2004. Evaluation of methods to reduce bacteria concentrations in spray-dried animal plasma and its effects on nursery pig performance. J Anim Sci 82, 250-261.
12
Fox, J.G., Barthold, S., Davisson, M., Newcomer, C.E., Quimby, F.W., Smith, A., 2006. The mouse in biomedical research, Academic Pr.
13
Furuta, M., Suwa, T., Kuwabara, Y., Otsuhata, K., Takeda, A., 2002. Electron-beam sterilization of laboratory animal diets--sterilizing effect of 10-MeV electrons from a linear accelerator. Exp Anim 51, 327-334.
14
Groesbeck, C.N., Derouchey, J.M., Tokach, M.D., Goodband, R.D., Dritz, S.S., Nelssen, J.L., 2009. Effects of irradiation of feed ingredients added to meal or pelleted diets on growth performance of weanling pigs. J Anim Sci 87, 3997-4002.
15
Hagiwara, A., Yoshino, H., Sano, M., Kawabe, M., Tamano, S., Sakaue, K., et al., 2005. Thirteen-week feeding study of thaumatin (a natural proteinaceous sweetener), sterilized by electron beam irradiation, in Sprague-Dawley rats. Food Chem Toxicol 43, 1297-1302.
16
Halls, N.A., Tallentire, A., 1978. Effects of processing and gamma irradiation on the microbiological contaminants of a laboratory animal diet. Lab Anim 12, 5-10.
17
Jorgensen, J.H., Ferraro, M.J., 2009. Antimicrobial susceptibility testing: a review of general principles and contemporary practices. Clin Infect Dis 49, 1749-1755.
18
Lee, J.-Y., Cho, S.-B., Kim, Y.-Y., Ohh, S.-J., 2010. Effect of gamma irradiation on nutrient digestibility in SPF mini-pig. Radiat Phys Chem 80, 123-124.
19
Morehouse, K.M., Komolprasert, V., 2004. Irradiation of food and packaging: an overview. ACS Publications.
20
National Research Council. Subcommittee on Laboratory Animal, N., 1995. Nutrient requirements of laboratory animals, National Academies Press.
21
Short, D.J., 1968. Animal Care Program of the Medical Research Council of Great Britain. Can Med Assoc J 98, 893-896.
22
Simas, M.M.S., Albuquerque, R., Oliveira, C.A., Rottinghaus, G.E., Correa, B., 2010. Influence of gamma radiation on productivity parameters of chicken fed mycotoxin-contaminated corn. Appl Radiat Isotopes 68, 1903-1908.
23
Wescott, R.B., Gardner, J.A., 1962. Apparatus and methods for the steam sterilization of feed for germfree laboratory animals. Technical manuscript 7.
24
ORIGINAL_ARTICLE
Scolicidal activity of Mesobuthus eupeus venom against the protoscolices of Echinococcus granulosus
Hydatidosis is an important zoonosis caused by a parasitic tapeworm, namely Echinococcus granulosus. This infection is distributed worldwide and affects the health as well as economic loss in both humans and animals. In most cases, the disease needs chemotherapy with or without surgery. Conventional drugs have some major problems, including drug complications, harmful side effects, and also progressive resistance. According to the importance of biological productions as alternative medicine, a large number of studies confirmed that whole venom and many peptide ingredients of the scorpion venom have various different medical benefits, including antimicrobial properties, due to the mechanism of blocking gated ion channel. In this study, the venom peptides of Mesobuthus eupeus scorpionwere purified using gel filtration chromatography and subsequently ion exchange chromatography, followed by the determination of the molecular weights of the proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) procedure. After collecting the hydatid cysts fluids from the liver of infected sheep, protoscolices were derived, washed, and encountered to the whole venom as well as eight different fractions of toxin 30, 60, 120, and 240 min after the exposure. In the next step, the viability of protoscolices was determined by eosin staining. The obtained results revealed that a venom fraction under 10 kDa killed all protoscolices after 30 min. Moreover, it was found that the scolicidal activity of fractions increases according to the time of exposure. As a result, it can be concluded that M. epeus venom peptides under its LD50 (1/2 LD50) can properly and quickly destroy the protoscolices of hydatid cysts at the level of applied concentrations and such components are good alternatives to treat hydatidosis.
https://archrazi.areeo.ac.ir/article_118932_27aa612b98153e6cb35fdab7db84339d.pdf
2019-06-01
183
189
10.22092/ari.2018.121416.1213
Hydatid cyst
Protoscolices
Mesobuthus eupeus
Venom
Treatment
H.
Jafari
hedieh_jafari@yahoo.com
1
Department of Venomous Animals and Toxins. Razi Vaccine and Serum Research Institute, Ahvaz, Agriculture Research, Education and Extension Organization, Ahvaz, Iran
LEAD_AUTHOR
M.
Nemati
nemati@yahoo.com
2
Department of Venomous Animals and Toxins. Razi Vaccine and Serum Research Institute, Ahvaz, Agriculture Research, Education and Extension Organization, Ahvaz, Iran
AUTHOR
P.
Haddad Molayan
haddad.p@gmail.com
3
Department of Pathobiology, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
AUTHOR
L.
Khaleghi Rostamkolaie
khalegi_l@yahoo.com
4
Department of Pathobiology, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
AUTHOR
H.
Hamidi Nejat
hamidinejat@yahoo.com
5
Department of Pathobiology, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran
AUTHOR
Baradaran, M., Jolodar, A., Jalali, A., Navidpour, S., Kafilzadeh, F., 2011. Sequence analysis of lysozyme C from the scorpion mesobuthus eupeus venom glands using semi-nested rt-PCR. Iran Red Crescent Med J 13, 719-725.
1
Borges, A., Silva, S., Op den Camp, H.J.M., Velasco, E., Alvarez, M., Alfonzo, M.J.M., et al., 2006. In vitro leishmanicidal activity of Tityus discrepans scorpion venom. Parasitol Res 99, 167-173.
2
Bygott, J.M., Chiodini, P.L., 2009. Praziquantel: Neglected drug? Ineffective treatment? Or therapeutic choice in cystic hydatid disease? Acta Tropica 111, 95-101.
3
Cao, L., Dai, C., Li, Z., Fan, Z., Song, Y., Wu, Y., et al.,
4
2012. Antibacterial Activity and Mechanism of a Scorpion Venom Peptide Derivative In Vitro and In Vivo. PLOS ONE 7, e40135.
5
Corzo, G., Escoubas, P., Villegas, E., Barnham, K.J., He, W., Norton, R.S., et al., 2001. Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator. Biochem J 359, 35.
6
El-Asmar, M.F., Swelam, N., Abdel Aal, T.M., Ghoneim, K., Hodhod, S.S., 1980. Factor(s) in the venom of scorpions toxic to Schistosoma mansoni (intestinal belharzia) cercariae. Toxicon 18, 711-715.
7
Feng, L., Gao, R., Gopalakrishnakone, P., 2008. Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi. Comp Biochem Physiol Part C: Toxicology & Pharmacology 148, 250-257.
8
Gao, B., Sherman, P., Luo, L., Bowie, J., Zhu, S., 2009. Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides.
9
Greenberg, R., 2005. Ca2+ signalling, voltage-gated Ca2+ channels and praziquantel in flatworm neuromusculature.
10
Guillaume, C., Deregnaucourt, C., Clavey, V., Schrével, J., 2004. Anti-Plasmodium properties of group IA, IB, IIA and III secreted phospholipases A2 are serum-dependent. Toxicon 43, 311-318.
11
Incamnoi, P., Patramanon, R., Thammasirirak, S., Chaveerach, A., Uawonggul, N., Sukprasert, S., et al., 2013. Heteromtoxin (HmTx), a novel heterodimeric phospholipase A2 from Heterometrus laoticus scorpion venom. Toxicon 61, 62-71.
12
Ito, A., Budke, C., 2017. The echinococcoses in Asia: The present situation.
13
Li, H., Shao, Y., Aji, T., Zhang, J., Kashif, K., Ma, Q., et al., 2014. Laparoscopic approach for total cystectomy in treating hepatic cystic echinococcosis. Parasite 21, 65.
14
Moerman, L., Bosteels, S., Noppe, W., Willems, J., Clynen, E., Schoofs, L., et al., 2002. Antibacterial and antifungal properties of α-helical, cationic peptides in the venom of scorpions from southern Africa. Eur J Biochem 269, 4799-4810.
15
Musaev, G.K., Fatyanova, A.S., Levkin, V.V., 2017. Principles and modern trends in liver echinococcosis treatment. Khirurgiia 12, 90-94.
16
Navidpour, S.H., Kovařík, F., Soleglad, M., Fet, V., 2008. Scorpions of Iran (Arachnida, Scorpiones) Part I Khoozestan Province. Euscorpius 65, 1-41.
17
Ortiz, E., Gurrola, G.B., Schwartz, E.F., Possani, L.D., 2015. Scorpion venom components as potential candidates for drug development. Toxicon 93, 125-135.
18
Oukkache, N., Chgoury, F., Lalaoui, M., Cano, A.A., Ghalim, N., 2013. Comparison between two methods of scorpion venom milking in Morocco. J Venom Anim Toxins Incl Trop Dis 19, 5.
19
Pérez-Serrano, J., Casado, N., Guillermo, Denegri, Rodriguez-Caabeiro, F., 1994. The effects of albendazole and albendazole sulphoxide combination-therapy on Echinococcus granulosus in vitro. Int J Parasitol 24, 219-224.
20
Perumal Samy, R., Stiles, B.G., Franco, O.L., Sethi, G., Lim, L.H.K., 2017. Animal venoms as antimicrobial agents. Biochem Pharmacol 134, 127-138.
21
Possani, L.D., Becerril, B., Delepierre, M., Tytgat, J., 1999. Scorpion toxins specific for Na+-channels. Eur J Biochem 264, 287-300.
22
Possani, L.D., Corona, M., Zurita, M., Rodrı́guez, M.H., 2002. From Noxiustoxin to Scorpine and Possible Transgenic Mosquitoes Resistant to Malaria. Arch Med Res 33, 398-404.
23
Shirmardi, S., Gandomkar, M., Shamsaei, M., Zare, A., Ghannadi Maragheh, M., Shafiei, M., et al., 2010. Preparation and Biodistribution Study of a 99mTc-Labeled Toxic Fraction of Iranian Mesobuthus Eupeus Scorpion Venom.
24
Smyth, J.D., Barrett, N.J., 1980. Procedures for testing the viability of human hydatid cysts following surgical removal, especially after chemotherapy. T Roy Soc Trop Med H 74, 649-652.
25
Thompson, R.C.A., 2017. Chapter Two - Biology and Systematics of Echinococcus. In: Thompson, R.C.A., Deplazes, P., Lymbery, A.J. (Eds.), Advances in Parasitology, Academic Press, pp. 65-109.
26
Urrea-París, M.A., Moreno, M.J., Casado, N., Rodriguez-Caabeiro, F., 2000. In vitro effect of praziquantel and albendazole combination therapy on the larval stage of Echinococcus granulosus. Parasitol Res 86, 957-964.
27
Wolstenholme, A.J., 2011. Ion channels and receptor as targets for the control of parasitic nematodes. Int J Parasitol: Drugs and Drug Resistance 1, 2-13.
28
Xu, Z.M., Li, Z.S., Wen, M.X., Peng, R.Y., Sun, L., Wu, X.Y., et al., 2008. In vitro effect of medicinal scorpion on the larvae of Ancylostoma caninum. Chinese J. Parasitol. Parasit. Dis 30, 387-391.
29
ORIGINAL_ARTICLE
Vasectomy in Mouse Model Using Electrosurgery Machine
Vasectomy in laboratory animals is a crucial step in the production of surrogate female mice. The surrogate mothers play a key role in successful embryo transfer, most important steps for the production of transgenic animal models, investigation of the preimplantation embryo development, and revitalization of cryopreserved strains. Abdominal and scrotal surgeries are common surgical procedures used in routine veterinary practice to produce vasectomized males. Two different surgical practice, namely electrosurgery and cold surgical practice, have been used as common techniques in operating rooms. Based on current knowledge, there is no published “technical note” as a detailed and step by step guideline to describe vasectomy using an electrosurgery machine (i.e., Bovie machine) in laboratory animal research and breeding facilities.The common problem during the laboratory animal surgery would be animal mortalities as a consequence of profound bleeding. The use of Bovie machine leads to the prevention of profound bleeding during the surgical practice.
https://archrazi.areeo.ac.ir/article_119159_a55b9bd5a29135ad42063a0973f0e7b9.pdf
2019-06-01
191
195
10.22092/ari.2019.126460.1345
Electrosurgery
Bovie Machine
Vasectomy
Embryo transfer
N.
Dadashpour Davachi
navid.d.davachi@gmail.com
1
Department of Research, Breeding and Production of Laboratory Animals, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
LEAD_AUTHOR
Aminimoghaddam, S., Pahlevani, R., Kazemi, M., 2018. Electrosurgery and clinical applications of electrosurgical devices in gynecologic procedures. Med J Islam Repub Iran 32, 90.
1
Baigrie, D., Badri, T., 2019. Electrosurgery. StatPearls, Treasure Island (FL).
2
Bermejo-Alvarez, P., Park, K.E., Telugu, B.P., 2014. Utero-tubal embryo transfer and vasectomy in the mouse model. J Vis Exp, e51214.
3
Charoenkwan, K., Iheozor-Ejiofor, Z., Rerkasem, K., Matovinovic, E., 2017. Scalpel versus electrosurgery for major abdominal incisions. Cochrane Database Syst Rev 6, CD005987.
4
Cheng, T.C., Huang, C.C., Huang, L.S., Chen, C.I., Lee, M.S., Liu, J.Y., 2004. Evaluation of mouse blastocyst implantation rate by morphology grading. Chin J Physiol 47, 43-47.
5
Ittner, L.M., Gotz, J., 2007. Pronuclear injection for the production of transgenic mice. Nat Protoc 2, 1206-1215.
6
Kolbe, T., Palme, R., Touma, C., Rulicke, T., 2012. Repeated use of surrogate mothers for embryo transfer in the mouse. Biol Reprod 86, 1-6.
7
Peneva, M., Gjorgjeska, A., Gjorgova, S.T., Dzonov, B., Noveski, L., Ginoski, V., et al., 2018. Evaluation of Pain Following the Use of Scalpel Versus Electrosurgery for Skin Incisions in the Facial Regions. Pril (Makedon Akad Nauk Umet Odd Med Nauki) 39, 107-112.
8
Scott, J.E., Swanson, E.A., Cooley, J., Wills, R.W., Pearce, E.C., 2017. Healing of canine skin incisions made with monopolar electrosurgery versus scalpel blade. Vet Surg 46, 520-529.
9
ORIGINAL_ARTICLE
First Case Report of an Unusual Echis genus (Squamata: Ophidia: Viperidae) Body Pattern Design in Iran
Three families of venomous snakes exist in Iran including Viperidae, Elapidae, and Hydrophidae. Viperidae family is the only family with a widespread distribution. Saw-scaled vipers are important poisonous snakes in Asia and Africa. This name is given to this snake due to the presence of obliquely keeled and serrated lateral body scales. Distribution of this genera is mostly reported in the central and southern regions of Iran. This genus has four main clades: the Echis carinatus, E. coloratus, E. ocellatus, and E. pyramidum. Design pattern in Echis species plays an important role in camouflage and variety of habitat. In the present report, we investigated a specimen from the eastern region of Iran; we examined 25 specimens of Echis that were collected from the eastern region of our country. Among them, only one specimen with a different pattern was found compared with the other 24 specimens by surveying meristic, mensural, and design pattern characters using valid key identifiers. The similarities between the specific Echis with a different pattern and other 24 specimens were also studied and compared. The results of this investigation clearly showed that although the pattern of the lateral white line and block on dorsal body of the specific Echis snake was different, since the meristic and mensural characters were similar to other Echis snakes it can be concluded that this specimen is not a different species; the difference in these patterns may be due to a minor genetic mutation of that specimen. It is the first case report of Echis carinatus sochureki Stemmler, 1969 from Iran with a different pattern.
https://archrazi.areeo.ac.ir/article_118719_5fe906af3cf8bf31d6222be66bb23d9a.pdf
2019-06-01
197
202
10.22092/ari.2018.115198.1145
Echis
Design pattern
Viperidae
Iran
S.
Navidpour
navid1038@hotmail.com
1
Department of Venomous animal and antivenom production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
A.
Salemi
crotalinae2010@gmail.com
2
Department of Venomous animal and antivenom production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
LEAD_AUTHOR
A.
Zare Mirakabadi
zareabbas83@gmail.com
3
Department of Venomous animal and antivenom production, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran
AUTHOR
Abbas Rhadi, F., Rastegar-Pouyani, N., Ghaleb Mohammed, R., Al-Fartosi, K.H., Browne, R.K., Karamiani, R., 2015. A Study of the Nomino typic Form of Saw Scaled Viper, Echis carinatus, (Schneider 1801), (Squamata: Ophidia: Viperidae) in Southern Iraq. Sch Acad J Biosci 3, 845-851.
1
Amr, Z., M Disi, A., 2011. Systematics, distribution and ecology of the snakes of Jordan.
2
Babocsay, G., 2003a. Geographic variation in Echis coloratus (Viperidae, Ophidia) in the Levant with the description of a new subspecies.
3
Babocsay, G., 2003b. A new species of saw‐scaled viper of the Echis coloratus complex (Ophidia: Viperidae) from Oman, Eastern Arabia. Syst Biodiver 1, 503-514.
4
Bagherian, A., Kami, H.G., 2009. On taxonomic status of the saw-scaled viper genus Echis (Viperidae: Reptilia) in Iran. Iranian Biology journal 21, 501-508.
5
Cherlin, V., 1981. The new saw-scaled viper Echis multisquamatus sp. nov. from southwestern and middle Asia. Proceedings of the Zoological Institute, Russ Ac Sc 101, 92-95.
6
Cherlin, V., Borkin, L., 1990. Taxonomic revision of the snake genus Echis (Viperidae): I, An analysis of the history of study and synonymy. Proceedings of the Zoological Institute, Russ Ac Sc 207, 175-192.
7
Latifi, M., 1991. Snakes of Iran, 2nd Edition. Tehran, Iran, Department of the Environment. Leviton, A.E., Anderson, S.C. (1970): The Amphibians and reptiles of Afghanistan, a checklist and key to the hrpetofauna. CAS 38, 163-206.
8
Lenk, P., Kalyabina, S., Wink, M., Joger, U., 2001. Evolutionary relationships among the true vipers (Reptilia: Viperidae) inferred from mitochondrial DNA sequences. Mol Phylogenet Evol 19, 94-104.
9
Mattison, C., 2014. Snakes and other reptiles and amphibians, DK, USA.
10
Mazuch, T., Hejduk, J., 2007. Zmije rodu Echis (Viperidae). Vydáno Českym Spolkem Pro Africkou Herpetologii.
11
Mohammadian, H., 2003. Reptiles & Amphibians of Iran. Shabpareh, Tehran, Iran,
12
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