آنالیز درون رایانه ای پروتین pMGA1.2 در سویه های واکسن و بیماریزای مایکوپلاسما گالی سپتیکوم
نالیز Insilico برای پروتئین pMGA1.2 در سویه های مایکوپلاسما گالی سپتیکوم
محورهای موضوعی : باکتری شناسی
فرزانه پورکریمی فتیده
1
,
مجید اسمعیلی زاد
2
,
محمد کارگر
3
,
مجید تبیانیان
4
,
فرشید کفیل زاده
5
1 - گروه میکروبیولوژی، واحد جهرم، دانشگاه آزاد اسلامی، جهرم، ایران.
2 - بخش تحقیق و توسعه، موسسه تحقیقات واکسن و سرم سازی رازی
3 - گروه میکروبیولوژی، دانشگاه آزاد اسلامی، واحد جهرم،
4 - بخش ایمونولوژی،موسسه تحقیقات و اکسن و سرم سازی رازی
5 - دانشگاه آزاد اسلامی، واحد جهرم، گروه میکروبیولوژی
کلید واژه: In silico, مایکوپلاسما گالی سپتیکوم, pMGA1.2 ,
چکیده مقاله :
زمینه و هدف: مایکوپلاسما گالی سپتیکوم، عامل بیماری مزمن تنفسی در جوجه های ماکیان، از نظر اقتصادی مهم ترین گونه مایکوپلاسما است که خسارات اقتصادی فراوان در سراسر جهان ایجاد می کند. فراوان ترین پروتئین های غشایی در مایکوپلاسما گالی سپتیکوم pMGA ، لیپوپروتئین هایی با حدود 67 کیلو دالتون می باشد. ژن‌های خانواده pMGA پتانسیل فوق‌العاده‌ای برای ایجاد تنوع در ساختار آنتی ژنی سطح سلول‌های مایکوپلاسما گالیسپتیکوم دارند. هدف از این مطالعه مقایسه الگوهای پروتئین pMGA بین سویه ها و میزبان های مختلف مایکوپلاسما گالی سپتیکوم بود. مواد و روش‌ها: ژنوم‌های کامل مایکوپلاسما گالیسپتیکوم در GenBank تا ژانویه 2020 بررسی و توالی‌های pMGA1.2 شناسایی، گروه‌بندی و کدگذاری شدند. پروتئین pMGA1.2 با طول 650 اسید آمینه بین دو میزبان مختلف (مرغ و فنچ خانگی) توسط نرم افزار بیوانفورماتیک در ژنوم های کامل مایکوپلاسما گالی سپتیکوم مورد بررسی قرار گرفت. یافته‌ها: ژن pMGA1.2 در سویه‌های مختلف مایکوپلاسما گالیسپتیکوم پنج گروه اصلی با بیش از 10 درصد واگرایی نشان داد. بر اساس تراز چند توالی، یک الگوی خاص در جدایه فنچ خانگی شناسایی شد. جالب توجه است که دو موتیف خاص 480DNQNVSNQ487 و SNVSSPSY647 639 درژن pMGA1.2 ازسویه TS-11 یافت شد که می تواند به عنوان نشانگر برای شناسایی و تمایز این سویه واکسن از مایکوپلاسما گالی سپتیکوم بیماری زا استفاده شود. نتیجه گیری: در این مطالعه نشان داده شد که پروتئین pMGA1.2 دارای نواحی آنتی ژنی اپی توپ سلول- B است که در تمام ایزوله ها حفظ شده است و می تواند در طراحی تست سرولوژیکی برای تشخیص آنتی بادی علیه مایکوپلاسما گالی سپتیکوم قابل استفاده باشد.
Background & Objectives: Mycoplasma gallisepticum, the pathogen responsible for chronic respiratory disease in chickens, is the most economically important species of Mycoplasma that causing tremendous economic losses worldwide. The most abundant membrane proteins in M. gallisepticum are pMGA, lipoproteins of about 67 kDa. The pMGA family genes have an extraordinary potential for diversifying antigenic structure on the surface of Mycoplasma gallisepticum cells. The aim of this study was to compare the pMGA protein patterns between different strains and hosts of Mycoplasma gallisepticum. Material & Methods: All Mycoplasma gallisepticum full genomes available in GenBank till January 2020 were considered and pMGA1.2 sequences were identified, grouped and coded. pMGA1.2 protein with a chain of 650 amino acids between two different hosts (poultry and house finch) was studied by bioinformatics software in all Mycoplasma gallisepticum full genomes. Results: pMGA1.2 gene among different strains of Mycoplasma gallisepticum showed five major groups with more than 10 percent divergence. Based on multiple sequence alignment, a specific pattern was identified in house finch isolates. Interestingly, two specific motifs 480DNQNVSNQ487 and 639SSNVSSPSY647 were found in the pMGA1.2 of TS-11 strain, which can probably be used as markers to identify and differentiate this vaccine strain from pathogenic Mycoplasma gallisepticum. Conclusion: This study showed that pMGA1.2 protein have some B-cell epitope antigenic regions that are conserved among all isolates and might be applicable to design serological test for detection antibody against Mycoplasma gallisepticum.
References
Mugunthan S.P, Kannan G, Chandra HM, Paital B. Infection, Transmission, Pathogenesisand Vaccine Development against Mycoplasma gallisepticum. Vaccines. 2023; 11: 469.
Swayne DE, Boulianne M, Logue CM, McDougald LR, Nair V, Suarez DL. Diseases of Poultry. 14th ed. Hoboken, NJ, USA.Wiley Blackwell; 2020: Volume 2, 907–923.
Dhondt A. A, Tessaglia D. L , Slothower R. L. Epidemic mycoplasmal conjunctivitis in house finches from eastern North America. Journal of Wildlife Diseases.1998; 34, 265–280.
Ley DH, Berkhoff JE, Levisohn S. Molecular epidemiologic investigations of Mycoplasma gallisepticum conjunctivitis in songbirds by random amplified polymorphic DNA analyses. Emerg Infect Dis.1997; 3:375–380.
Dhondt AA, Tessaglia DL, Slothower RL. Epidemic mycoplasmal conjunctivitis in house finches from eastern North America. Journal of Wildlife Diseases.1998; 34: 265–280.
Dhondt AA, DeCoste JC, Ley DH, Hochachk WM. Diverse wild bird host range of Mycoplasma gallisepticum in eastern North America. PLoS One. 2014; 9:e103553.
Ter Veen C, Dijkman R, De Wit JJ, Gyuranecz M, Feberwee A. Decrease of Mycoplasma gallisepticum seroprevalence and introduction of new genotypes in Dutch commercial poultry during the years 2001-2018. Avian Pathology. 2021; 50: 52-60.
Wanasawaeng Wisanu, Chaichote Supawadee, Chansiripornchai Niwat. Deveolpment of ELISA and serum plate agglutination for detecting antibodies of Mycoplasma gallisepticum using strain of Thai isolate.Thai J Vet Med. 2015;45(4):499-507.
. Hnatow LL, Keeler CL Jr, Tessmer LL, Czymmek K, Dohms JE. Characterization of MGC2 a Mycoplasma gallisepticum cytadhesin with homology to the Mycoplasma pneumoniae 30-kilodalton protein P30 and Mycoplasma genitalium P32. Infect Immun.1998; 66: 3436–3442.
Chen H, Yu S, Shen X, Chen D, Qiu X, Song C, Ding C. The Mycoplasma gallisepticum alpha-enolase is cell surface-exposed and mediates adherence by binding to chicken plasminogen. Microb Pathog .2011; 51:285–290.
Athamna A, Rosengarten R, Levisohn S, Kahane I, Yogev D. Adherence of Mycoplasma gallisepticum involves variable surface membrane proteins. Infect Immun .1997; 65: 2468–2471.
Markham PF, Glew MD, Whithear KG, Walker ID. Molecular cloning of a gene family that encodes pMGA, a hemagglutinin of Mycoplasma gallisepticum. Infect Immun.1993; 61: 903–909.
Chambaud I, Wróblewski H, Blanchard A. Interactions between mycoplasma lipoproteins and the host immune system.Trends Microbiol .1999; 7:493–499.
Baseggio N, Glew MD, Markham PF, Whithear KG , Browning GF. Size and genomic location of the pMGA multigene family of Mycoplasma gallisepticum. Microbiology.1996; 142: 1429-1435.
. Czifra G, Tuboly T, Sundquist BG, Stipkovits L. Monoclonal antibodies to Mycoplasma gallisepticum membrane proteins. Avian Dis.1993; 37:689–696.
Garcı´a M, Elfaki MG, Kleven SH. Analysis of the variability in expression of Mycoplasma gallisepticum surface antigens. Vet Microbiol.1994; 42:147–158.
Forsyth MH, Tourtelotte ME, Geary SJ. Localization of an immunodominant 64-kDa lipoprotein (LP64) in the membrane of Mycoplasma gallisepticum and its role in cytadherence. Mol Microbiol. 1992; 6: 2099–2106.
Carpenter TE, Mallinson ET, Miller KF, Gentry RF, Schwartz LD. Vaccination with F-strain Mycoplasma gallisepticum to reduce production losses in layer chickens. Avian Dis. 1981; 25:404–409.
Noormohammadi AH, Whithear KG. Comparison of the short-term and long-term efficacies of the Mycoplasma gallisepticum vaccines ts-11 and 6/85. Avian Pathology. 2019; 48: 238-244.
. Noormohammadi AH, Markham PF, Duffy MF, Whithear KG, Browning GF. Multigene families encoding the major hemagglutinins in phylogenetically distinct Mycoplasmas. ASM J Infection and Immunity.1998; 66 (7):3470-3475.
Febrwee A, Dewit S, Dijkman R. Clinical expression, epidemiology and monitoring of Mycoplasma gallisepticum and Mycoplasma synoviae: an update. Avian Pathology. 2021; 1-61.
Bermudez AJ, Kalbac M. Control of Mycoplasma gallisepticum infection in commercial layers: A field study. J Am Vet Med Assoc. 1988; 192:1783.
Glew, MD, Markham PF, Browning GF, Walker ID. Expression studies on four members of the pMGA multigene family in Mycoplasma gallisepticum. Microbiology.1995; 141: 3005–3014.
Baseggio N, Glew MD, Markham PF, Whithear KG, Browning GF. Size and genomic location of the pMGA multigene family of Mycoplasma gallisepticum. Microbiology.1996; 142: 1429–1435.
Kay BK, Williamson MP, Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 2000; 14:231-241.
Liu L, Payne DM, van Santen VL, Dybvig K, Panangala VS. A protein (M9) associated with monoclonal antibody mediated agglutination of Mycoplasma gallisepticum is a member of the pMGA family. Infect Immun. 1998; 66: 5570-5575.
Markham PF, Glew MD, Brandon MR, Walker ID, Whithear KG. Characterization of a major hemagglutinin protein from Mycoplasma gallisepticum. Infect Immun.1992; 60:3885–3891.
Yasmin F, Ideris A, Omar AR, Bejo MH, Islam R, Wei TS, Giap TC. Molecular characterization of field strains of Mycoplasma gallisepticum in Malaysia through pMGA and pVPA genes sequencing. Cogent Biology. 2018; 4:1456738
Glew MD, Baseggio N, Markham PF, Browning GF, Walker ID. Expression of the pMGA genes of Mycoplasma gallisepticum is controlled by variation in the GAA trinucleotide repeat lengths within the 5`noncoding regions. Infect Immun.1998; 66: 5833-5841.
Ley DH. Mycoplasma gallisepticum infection. In: Saif YM, Barnes HJ, Glisson JR, Fadly AM, Mc Dougald LR, Swayne DE . Diseases of poultry. 11 th ed. Lowa State Press, Ames, IA; 2003:722-744.
Javid H. Antigenic properties of Finegoldia magna protein L and Type IV pilin (pilA) for in-silico multi epitope peptide vaccine designing. JMW. 2020; 42(1):78-98[In Persion]
Souod N, Kargar M, Hoseini MH, Jafarinia M. Designing, cloning and expression of ctx-B-tcpA-c-cpe gene in E.coli as a cholera vaccine candidate. JMW. 2021;14(1):6-20[In Persion]
Shahbaaz M, Bisetty K, Ahmad F, Hassan MI. In silico approaches for the identification of virulence candidates amongst hypothetical proteins of Mycoplasma pneumonia. Comput Biol Chem. 2015; 59 Pt A: 67–80.
Gaurivaud P, Baranowski E, Pau-Roblot C, Sagné E, Citti C, Tardy F. Mycoplasma agalactiae Secretion of β-(1→6)-Glucan, a Rare Polysaccharide in Prokaryotes, Is Governed by High-Frequency Phase Variation. Appl Environ Microbiol. 2016; 82:370–3383.
Mugunthan SP, Chandra HM. A computational reverse vaccinology approach for the design and development of multi-epitopic vaccine against avian pathogen Mycoplasma gallisepticum. Front Vet Sci. 2021; 8:721061.
Mugunthan SP and Chandra HM. In silico structural homology modeling and functional characterization of Mycoplasma gallisepticum variable lipoprotein hemagglutin proteins. Front Vet Sci. 2022; 9: 943831.