Computational Identification and Characterization of a Promiscuous T-Cell Epitope on the Extracellular Protein 85B of Mycobacterium spp. for Peptide-Based Subunit Vaccine DesignReportar como inadecuado




Computational Identification and Characterization of a Promiscuous T-Cell Epitope on the Extracellular Protein 85B of Mycobacterium spp. for Peptide-Based Subunit Vaccine Design - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

BioMed Research International - Volume 2017 2017, Article ID 4826030, 14 pages - https:-doi.org-10.1155-2017-4826030

Research Article

Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan

Department of Genetic Engineering and Biotechnology, Shahjalal University of Science and Technology, Sylhet 3114, Bangladesh

Department of Dermatology, Sylhet Women’s Medical College, Sylhet 3114, Bangladesh

Correspondence should be addressed to Abul Kalam Azad

Received 25 October 2016; Revised 25 January 2017; Accepted 26 February 2017; Published 16 March 2017

Academic Editor: Marcela I. Henao-Tamayo

Copyright © 2017 Md. Saddam Hossain et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Tuberculosis TB is a reemerging disease that remains as a leading cause of morbidity and mortality in humans. To identify and characterize a T-cell epitope suitable for vaccine design, we have utilized the Vaxign server to assess all antigenic proteins of Mycobacterium spp. recorded to date in the Protegen database. We found that the extracellular protein 85B displayed the most robust antigenicity among the proteins identified. Computational tools for identifying T-cell epitopes predicted an epitope, 181-QQFIYAGSLSALLDP-195, that could bind to at least 13 major histocompatibility complexes, revealing the promiscuous nature of the epitope. Molecular docking simulation demonstrated that the epitope could bind to the binding groove of MHC II and MHC I molecules by several hydrogen bonds. Molecular docking analysis further revealed that the epitope had a distinctive binding pattern to all DRB1 and A and B series of MHC molecules and presented almost no polymorphism in its binding site. Moreover, using -Allele Frequency Database,- we checked the frequency of HLA alleles in the worldwide population and found a higher frequency of both class I and II HLA alleles in individuals living in TB-endemic regions. Our results indicate that the identified peptide might be a universal candidate to produce an efficient epitope-based vaccine for TB.





Autor: Md. Saddam Hossain, Abul Kalam Azad, Parveen Afroz Chowdhury, and Mamoru Wakayama

Fuente: https://www.hindawi.com/



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