{"title":"X-Ray Crystallography Based Epitope Mapping of Glycoproteins and RNA in Chandipura Vesiculovirus for Vaccine Design.","authors":"Aron Rodrick Lakra","doi":"10.1111/imm.13907","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":13508,"journal":{"name":"Immunology","volume":" ","pages":""},"PeriodicalIF":4.9000,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Immunology","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1111/imm.13907","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"IMMUNOLOGY","Score":null,"Total":0}
引用次数: 0
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.
期刊介绍：
Immunology is one of the longest-established immunology journals and is recognised as one of the leading journals in its field. We have global representation in authors, editors and reviewers.
Immunology publishes papers describing original findings in all areas of cellular and molecular immunology. High-quality original articles describing mechanistic insights into fundamental aspects of the immune system are welcome. Topics of interest to the journal include: immune cell development, cancer immunology, systems immunology/omics and informatics, inflammation, immunometabolism, immunology of infection, microbiota and immunity, mucosal immunology, and neuroimmunology.
The journal also publishes commissioned review articles on subjects of topical interest to immunologists, and commissions in-depth review series: themed sets of review articles which take a 360° view of select topics at the heart of immunological research.
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