In silico prediction of the epitopes for the immunogenic proteins present in Mycobacterium avium subsp. paratuberculosis

D SWATHI; S SARANYA; A RAJA; K VIJAYARANI; K KUMANAN

doi:10.56093/ijans.v90i2.98766

Authors

D SWATHI Tamil Nadu Veterinary and Animal Sciences University, Chennai, Tamil Nadu 600 051 India
S SARANYA Tamil Nadu Veterinary and Animal Sciences University, Chennai, Tamil Nadu 600 051 India
A RAJA Tamil Nadu Veterinary and Animal Sciences University, Chennai, Tamil Nadu 600 051 India
K VIJAYARANI Professor and Head, Tamil Nadu Veterinary and Animal Sciences University, Chennai, Tamil Nadu 600 051 India
K KUMANAN Professor and Head, Tamil Nadu Veterinary and Animal Sciences University, Chennai, Tamil Nadu 600 051 India

https://doi.org/10.56093/ijans.v90i2.98766

Keywords:

Immunogenic proteins, 3D modeling, Mycobaterium avium, T cell Epitopes, ZDock

Abstract

Johneâ€™s disease caused by Mycobacterium avium subsp. paratuberculosis is a widespread problem in ruminants worldwide. Diagnosis of the disease during the early stages of infection is difficult. In search of newer proteins with antigenic and immunogenic characters, in silico epitope analysis of the immunogenic proteins was performed which identifies the proteins expressed during the early stages of infection and which could stimulate cell mediated immune response. T cell epitopes were predicted for the six immunogenic proteins and the epitopes were sorted based on the percentile ranking and repetition among MHC Class I alleles. 3D modeling and protein-protein interaction studies revealed that ELPLPQTYVD, DVVGYDRTQD, PDLQSVLGATPGAG, DGLRAQDD, DGLRAQDD and PGHVTDD epitopes interact with the MHC Class I molecule through hydrogen bonding. These epitopes are identified as potent candidates for the immunodiagnostic studies and could be further evaluated using in vitro studies.

Downloads

Download data is not yet available.

References

Amigorena S and Savina A. 2010. Intracellular mechanisms of antigen cross presentation in dendritic cells. Current Opinion in Immunology 22: 109–117. DOI: https://doi.org/10.1016/j.coi.2010.01.022

Bhutediya J M, Dandapat P, Chakrabarty A, Das R, Nanda P K, Bandyopadhyay S and Biswas T K. 2017. Prevalence of paratuberculosis in organized and unorganized dairy cattle herds in West Bengal, India. Veterinary World 10(6): 574. DOI: https://doi.org/10.14202/vetworld.2017.574-579

Carlos P, Roupie V, Holbert S, Ascencio F, Huygen K, Gomez- Anduro G, Branger M, Reyes-Becerril M and Angulo C. 2015. In silico epitope analysis of unique and membrane associated proteins from Mycobacterium avium subsp. paratuberculosis for immunogenicity and vaccine evaluation. Journal of Theoretical Biology 384: 1–9. DOI: https://doi.org/10.1016/j.jtbi.2015.08.003

Eisen H N, Hou X H, Shen C, Wang K, Tanguturi V K, Smith C, Kozyrytska K, Nambiar L, McKinley C A, Chen J and Cohen R J. 2012. Promiscuous binding of extracellular peptides to cell surface class I MHC protein. Proceedings of the National Academy of Sciences 109: 4580–85. DOI: https://doi.org/10.1073/pnas.1201586109

Gurung R B, Purdie A C, Begg D J and Whittington R J. 2012. In silico identification of epitopes inMycobacterium avium subsp paratuberculosis proteins that were upregulated under stress conditions. Clinical and Vaccine Immunology 19(6): 855–64. DOI: https://doi.org/10.1128/CVI.00114-12

Harris N B and Barletta R G. 2001. Mycobacterium avium subsp. paratuberculosis in veterinary medicine. Clinical Microbiology Reviews 14: 489–512. DOI: https://doi.org/10.1128/CMR.14.3.489-512.2001

Hatherley R, Brown D K, Glenister M and Bishop O T. 2016. PRIMO: An interactive homology modeling pipeline. PLoS ONE 11(11): e0166698. DOI: https://doi.org/10.1371/journal.pone.0166698

Hoek A, Rutten V P, Van der Zee R, Davies C J and Koets A P. 2010. Epitopes of Mycobacterium avium sp. paratuberculosis 70 kDa heat-shock protein activate bovine helper T cells in outbred cattle. Vaccine 28: 5910–19. DOI: https://doi.org/10.1016/j.vaccine.2010.06.042

Jeffrey G A and Jeffrey G A. 1997. An introduction to hydrogen bonding. Oxford University Press, New York.

Kawaji S, Gumber S and Whittington R J. 2012. Evaluation of the immunogenicity of Mycobacterium avium subsp. paratuberculosis (MAP) stress-associated recombinant proteins. Veterinary Microbiology 155: 298–309. DOI: https://doi.org/10.1016/j.vetmic.2011.08.021

Ramachandran G T and Sasisekharan V. 1968. Conformation of polypeptides and proteins. Advances in Protein Chemistry 23: 283–437. DOI: https://doi.org/10.1016/S0065-3233(08)60402-7

Rana A and Akhter Y. 2016. A multi-subunit based, thermodynamically stable model vaccine using combined immunoinformatics and protein structure based approach. Immunobiology 221: 544–57. DOI: https://doi.org/10.1016/j.imbio.2015.12.004

Stabel J R. 2000. Transitions in immune responses to Mycobacterium paratuberculosis. Veterinary Microbiology 77: 465–73. DOI: https://doi.org/10.1016/S0378-1135(00)00331-X