Computer aided prediction and identification of potential epitopes in the receptor binding domain (RBD) of spike (S) glycoprotein of MERS-CoV |
| |
Authors: | Mohammad Tuhin ali Mohammed Monzur Morshed Md Amran Gazi Md Abu Musa Md Golam Kibria Md Jashim Uddin Md Anik Ashfaq Khan Shihab Hasan |
| |
Institution: | 1.Department of Biochemistry and Molecular Biology, University of Dhaka, Bangladesh;2.Laboratory Science Division, International Centre for Diarrhoeal Disease Research, Dhaka, Bangladesh;3.Department of Genetic Engineering and Biotechnology, Shahjalal University of Science and Technology, Sylhet, Bangladesh;4.Bioinformatics Lab, QIMR Berghofer Medical Research Institute, Brisbane, Queensland, Australia;5.School of Medicine, The University of Queensland (UQ), Brisbane, Queensland, Australia |
| |
Abstract: | Middle East Respiratory Syndrome Coronavirus (MERS-CoV) belongs to the coronaviridae family. In spite of several outbreaks in
the very recent years, no vaccine against this deadly virus is developed yet. In this study, the receptor binding domain (RBD) of
Spike (S) glycoprotein of MERS-CoV was analyzed through Computational Immunology approach to identify the antigenic
determinants (epitopes). In order to do so, the sequences of S glycoprotein that belong to different geographical regions were
aligned to observe the conservancy of MERS-CoV RBD. The immune parameters of this region were determined using different in
silico tools and Immune Epitope Database (IEDB). Molecular docking study was also employed to check the affinity of the potential
epitope towards the binding cleft of the specific HLA allele. The N-terminus RBD (S367-S606) of S glycoprotein was found to be
conserved among all the available strains of MERS-CoV. Based on the lower IC50 value, a total of eight potential T-cell epitopes and
19 major histocompatibility complex (MHC) class-I alleles were identified for this conserved region. A 9-mer epitope CYSSLILDY
displayed interactions with the maximum number of MHC class-I molecules and projected the highest peak in the B-cell
antigenicity plot which concludes that it could be a better choice for designing an epitope based peptide vaccine against MERSCoV
considering that it must undergo further in vitro and in vivo experiments. Moreover, in molecular docking study, this epitope
was found to have a significant binding affinity of -8.5 kcal/mol towards the binding cleft of the HLA-C*12:03 molecule. |
| |
Keywords: | Epitope HLA ligand MERS-CoV Receptor Binding Domain Spike glycoprotein |
|
|