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Intraspecies Gene Variation within Putative Epitopes of Immunodominant Protein P48 of Mycoplasma agalactiae | ||
| Archives of Razi Institute | ||
| مقاله 2، دوره 73، شماره 4، اسفند 2018، صفحه 265-275 اصل مقاله (973.56 K) | ||
| نوع مقاله: Original Articles | ||
| شناسه دیجیتال (DOI): 10.22092/ari.2017.115059.1143 | ||
| نویسندگان | ||
| P. Panahi1؛ S. A. Pourbakhsh* 1؛ T. Zahraei Salehi2؛ M. Esmaelizad3؛ R. Madani4، 5 | ||
| 1Mycoplasma Reference Laboratory, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran | ||
| 2Department of Microbiology and Immunology, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran | ||
| 3Central Laboratory Department, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran | ||
| 4Proteomics and Biochemistry Department, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran. | ||
| 5Department of Microbiology, School of Specialized Veterinary Science, Science and Research Branch, Islamic Azad University, Tehran, Iran. | ||
| چکیده | ||
| P48 protein of Mycoplasma agalactiae is used to diagnose infection and was identified as potential vaccine candidate. According to the genetic nature of mycoplasma and variable sensitivity in P48-based serological diagnosis tests, intra species variation of P48 nucleotide sequence investigated in 13 field isolates of difference province of Iran along with three vaccine strains. Samples were collected from sheep and goat and were cultured in modified PPLO broth. Two pair of primer employed to confirm genus and species of isolates and a pair of primer has developed to amplify the P48 gene. The sequencing results of PCR products were aligned and analyzed besides published sequences in GenBank. T-Cell and B-Cell epitopes and antigenicity of sequence were computationally predicted. The results have shown P48 nucleotide sequences are 99.9% identical in field isolates and vaccine strain of Iran, but analysis of GenBank published sequences have shown divergence up to 5.3% at the nucleotide level and up to 4.9% divergence in protein level of P48 sequences of Iran isolates and other available sequences in GenBank. Single nucleotide polymorphism exists in 89 positions and variable amino acid was observed at 25 residues. Phylogenetic analyses have shown that Mycoplasma agalactiae isolates fall into three main groups based on P48 nucleotide sequences. Immunoinformatics analysis of all available P48 nucleotide sequences have revealed that gene variation lead to differences in immunological properties, but the gene in Iranian isolates are conservative and stable. The sequence variation in epitopes can be underlying source of antigen heterogeneity as a result, affect serological tests accuracy. Due to the high level of divergence in worldwide isolates and high degree of similarity in P48 protein of Iranian isolates, designing recombinant P48 protein based on local pattern can increase the sensitivity and consistency of serological test. | ||
| کلیدواژه‌ها | ||
| Mycoplasma؛ Contagious Agalactiae؛ P48؛ Variation؛ Antigen Heterogeneity | ||
| عنوان مقاله [English] | ||
| .. | ||
| کلیدواژه‌ها [English] | ||
| مایکوپلاسما, آگالاکسی مسری, P48, تنوع, تنوع آنتی ژنی | ||
| مراجع | ||
|
Abtin, A.R., Pourbakhsh, S.A., Ashtari, A., Bayatzadeh, M.A., Barani, S.M., Ahangaran, S., 2013. Isolation and identification of Mycoplasma agalactiae by culture and polymerase chain reaction (PCR) from sheep of Qom province, Iran. Archives of Razi Institute 68, 11-16.
Alberti, A., Robino, P., Chessa, B., Rosati, S., Addis, M.F., Mercier, P., et al., 2008. Characterisation of Mycoplasma capricolum P60 surface lipoprotein and its evaluation in a recombinant ELISA. Veterinary microbiology 128, 81-89.
Alexander, H., Alexander, S., Getzoff, E.D., Tainer, J.A., Geysen, H.M., Lerner, R.A., 1992. Altering the antigenicity of proteins. Proceedings of the National Academy of Sciences 89, 3352-3356.
Bergonier, D., De Simone, F., Russo, P., Solsona, M., Lambert, M., Poumarat, F., 1996. Variable expression and geographic distribution of Mycoplasma agalactiae surface epitopes demonstrated with monoclonal antibodies. FEMS microbiology letters 143, 159-165.
Carvalho, F.M., Fonseca, M.M., De Medeiros, S.B., Scortecci, K.C., Blaha, C.A.G., Agnez-Lima, L.F., 2005. DNA repair in reduced genome: the Mycoplasma model. Gene 360, 111-119.
Chessa, B., Pittau, M., Puricelli, M., Zobba, R., Coradduzza, E., Dall’Ara, P., et al., 2009. Genetic immunization with the immunodominant antigen P48 of Mycoplasma agalactiae stimulates a mixed adaptive immune response in BALBc mice. Research in veterinary science 86, 414-420.
Citti, C., Nouvel, L.-X., Baranowski, E., 2010. Phase and antigenic variation in mycoplasmas. Future microbiology 5, 1073-1085.
Deitsch, K.W., Lukehart, S.A., Stringer, J.R., 2009. Common strategies for antigenic variation by bacterial, fungal and protozoan pathogens. Nature reviews. Microbiology 7, 493.
Fusco, M., Corona, L., Onni, T., Marras, E., Longheu, C., Idini, G., et al., 2007. Development of a sensitive and specific enzyme-linked immunosorbent assay based on recombinant antigens for rapid detection of antibodies against Mycoplasma agalactiae in sheep. Clinical and Vaccine Immunology 14, 420-425.
Glew, M.D., Marenda, M., Rosengarten, R., Citti, C., 2002. Surface diversity in Mycoplasma agalactiae is driven by site-specific DNA inversions within the vpma multigene locus. Journal of bacteriology 184, 5987-5998.
Khan, L.A., Loria, G.R., Ramirez, A.S., Nicholas, R.A., Miles, R.J., Fielder, M.D., 2005. Biochemical characterisation of some nonfermenting, nonarginine hydrolysing mycoplasmas of ruminants. Veterinary microbiology 109, 129-134.
Kojima, A., Takahashi, T., Kijima, M., Ogikubo, Y., Nishimura, M., Nishimura, S., et al., 1997. Detection of Mycoplasmain Avian Live Virus Vaccines by Polymerase Chain Reaction. Biologicals 25, 365-371.
Komar, A.A., Lesnik, T., Reiss, C., 1999. Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS letters 462, 387-391.
Leslie, A., Pfafferott, K., Chetty, P., Draenert, R., Addo, M., Feeney, M., et al., 2004. HIV evolution: CTL escape mutation and reversion after transmission. Nature medicine 10, 282-289.
Nicholas, R., Ayling, R., McAuliffe, L., 2009. Vaccines for Mycoplasma diseases in animals and man. Journal of comparative pathology 140, 85-96.
Nouvel, L.X., Sirand-Pugnet, P., Marenda, M.S., Sagné, E., Barbe, V., Mangenot, S., et al., 2010. Comparative genomic and proteomic analyses of two Mycoplasma agalactiae strains: clues to the macro-and micro-events that are shaping mycoplasma diversity. BMC genomics 11, 86.
Nyvold, C., Birkelund, S., Christiansen, G., 1997. The Mycoplasma hominis P120 membrane protein contains a 216 amino acid hypervariable domain that is recognized by the human humoral immune response. Microbiology 143, 675-688.
Oravcová, K., López-Enríquez, L., Rodríguez-Lázaro, D., Hernández, M., 2009. Mycoplasma agalactiae p40 gene, a novel marker for diagnosis of contagious agalactia in sheep by real-time PCR: assessment of analytical performance and in-house validation using naturally contaminated milk samples. Journal of clinical microbiology 47, 445-450.
Palmer, G.H., Bankhead, T., Seifert, H.S., 2016. Antigenic variation in bacterial pathogens. Microbiology spectrum 4.
Poumarat, F., Le Grand, D., Gaurivaud, P., Gay, E., Chazel, M., Game, Y., et al., 2012. Comparative assessment of two commonly used commercial ELISA tests for the serological diagnosis of contagious agalactia of small ruminants caused by Mycoplasma agalactiae. BMC veterinary research 8, 109.
Razin, S., Yogev, D., Naot, Y., 1998. Molecular biology and pathogenicity of mycoplasmas. Microbiology and Molecular Biology Reviews 62, 1094-1156.
Rosati, S., Pozzi, S., Robino, P., Montinaro, B., Conti, A., Fadda, M., et al., 1999. P48 major surface antigen of Mycoplasma agalactiae is homologous to a malp product of Mycoplasma fermentans and belongs to a selected family of bacterial lipoproteins. Infection and immunity 67, 6213-6216.
Rosati, S., Robino, P., Fadda, M., Pozzi, S., Mannelli, A., Pittau, M., 2000. Expression and antigenic characterization of recombinant Mycoplasma agalactiae P48 major surface protein. Veterinary microbiology 71, 201-210.
Rosengarten, R., Behrens, A., Stetefeld, A., Heller, M., Ahrens, M., Sachse, K., et al., 1994. Antigen heterogeneity among isolates of Mycoplasma bovis is generated by high-frequency variation of diverse membrane surface proteins. Infection and immunity 62, 5066-5074.
Rosengarten, R., Yogev, D., 1996. Variant colony surface antigenic phenotypes within mycoplasma strain populations: implications for species identification and strain standardization. Journal of clinical microbiology 34, 149-158.
Stear, M., 2005. OIE Manual of Diagnostic Tests and Vaccines for Terrestrial Animals (Mammals, Birds and Bees) 5th Edn. Volumes 1 & 2. World Organization for Animal Health 2004. ISBN 92 9044 622. Cambridge Univ Press.
Tola, S., Angioi, A., Rocchigiani, A., Idini, G., Manunta, D., Galleri, G., et al., 1997a. Detection of Mycoplasma agalactiae in sheep milk samples by polymerase chain reaction. Veterinary microbiology 54, 17-22. Tola, S., Crobeddu, S., Chessa, G., Uzzau, S., Idini, G., Ibba, B., et al., 2001. Sequence, cloning, expression and characterisation of the 81‐kDa surface membrane protein (P80) of Mycoplasma agalactiae. FEMS microbiology letters 202, 45-50.
Tola, S., Manunta, D., Cocco, M., Turrini, F., Rocchigiani, A.M., Idini, G., et al., 1997b. Characterization of membrane surface proteins of Mycoplasma agalactiae during natural infection. FEMS microbiology letters 154, 355-362.
Wang, H., Bian, T., Merrill, S.J., Eckels, D.D., 2002. Sequence variation in the gene encoding the nonstructural 3 protein of hepatitis C virus: evidence for immune selection. Journal of molecular evolution 54, 465-473.
Williams, L.E., Wernegreen, J.J., 2013. Sequence context of indel mutations and their effect on protein evolution in a bacterial endosymbiont. Genome biology and evolution 5, 599-605.
Ziegler, S., Skibbe, K., Walker, A., Ke, X., Heinemann, F.M., Heinold, A., et al., 2014. Impact of sequence variation in a dominant HLA-A* 02-restricted epitope in hepatitis C virus on priming and cross-reactivity of CD8+ T cells. Journal of virology 88, 11080-11090. | ||
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