X‐Ray Crystallography Based Epitope Mapping of Glycoproteins and <scp>RNA</scp> in Chandipura Vesiculovirus for Vaccine Design

This study investigates potential epitopes in the glycoprotein and RNA of Chandipura vesiculovirus (CHPV) using MHC Class I (HLA-A0201) and MHC Class II (DRB1_0101) molecules with 3D structures derived from x-ray crystallography. Computationally derived peptides were mapped and subjected to in silico docking, revealing promising targets for CD8+ cytotoxic and CD4+ helper T cells. Key factors analysed include solvent accessible surface area (SASA), Debye-Waller factor (B-factor), and polar bond interactions. Post-docking, removal of N-acetylglucosamine (NAG) increased peptide stability and reduced B-factors, while SO4 presence had minimal impact. SASA values increased by up to 237.5% with MHC Class I, and RNA docking with MHC Class II displayed mixed SASA changes. Polar bond interactions also increased post-docking, indicating the strong potential of identified CHPV epitopes.

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Publication Details

Journal
Immunology
Published
2025-02-04
DOI
https://doi.org/10.1111/imm.13907
Primary Topic
Virology and Viral Diseases
Type
article
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article

X‐Ray Crystallography Based Epitope Mapping of Glycoproteins and RNA in Chandipura Vesiculovirus for Vaccine Design

Aron Rodrick Lakra
Immunology
Virology and Viral Diseases
article

X‐Ray Crystallography Based Epitope Mapping of Glycoproteins and RNA in Chandipura Vesiculovirus for Vaccine Design

Aron Rodrick Lakra
article en

Abstract

This study investigates potential epitopes in the glycoprotein and RNA of Chandipura vesiculovirus (CHPV) using MHC Class I (HLA-A0201) and MHC Class II (DRB1_0101) molecules with 3D structures derived from x-ray crystallography. Computationally derived peptides were mapped and subjected to in silico docking, revealing promising targets for CD8+ cytotoxic and CD4+ helper T cells. Key factors analysed include solvent accessible surface area (SASA), Debye-Waller factor (B-factor), and polar bond interactions. Post-docking, removal of N-acetylglucosamine (NAG) increased peptide stability and reduced B-factors, while SO4 presence had minimal impact. SASA values increased by up to 237.5% with MHC Class I, and RNA docking with MHC Class II displayed mixed SASA changes. Polar bond interactions also increased post-docking, indicating the strong potential of identified CHPV epitopes.

ImmunologyVol. 175(1)
Openalex Percentile: Top 97%
Virology and Viral Diseases
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