Changes in the dynamic characteristics of G-protein can alter the immune-protection efficacy of rabies virus vaccine

N-glycosylation of rabies virus glycoprotein dynamically regulates protein folding, stability, and antigenicity. Therefore, regulation of N-glycan modification is key to improving vaccine stability and protective efficacy. How the type and modification sites of N-glycans affect the protective efficacy of rabies vaccines remains unclear. Our research indicates that there are differences in the protective efficacy of rabies virus G-proteins modified with different N-glycans. Moreover, the modification of the three-branched hybrid glycan at the aa 319 site of G-protein significantly altered the hydrophobicity, flexibility, and radius, and increased its trimeric antigen instability through molecular dynamics demonstrations. These findings update the current understanding of the impact of glycans on vaccine antigenicity and develop a system to evaluate the stability of antigen glycoproteins based on molecular dynamics.

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Publication Details

Journal
Journal of Virology
Published
2025-02-21
DOI
https://doi.org/10.1128/jvi.01954-24
Citations
2
Primary Topic
Rabies epidemiology and control
Type
article
Field-Weighted Citation Impact
2.07
Controls
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article

Changes in the dynamic characteristics of G-protein can alter the immune-protection efficacy of rabies virus vaccine

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2 citations
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Rabies epidemiology and control
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Changes in the dynamic characteristics of G-protein can alter the immune-protection efficacy of rabies virus vaccine

Xiang Hong, Leitai Shi, Shen Dong, Wen Su, Yu Gao, Donglan Liu, Changxu Chen, Liteng Yang, Binlei Liu, Yang Zhang, Fan Wu, Wenzhi He, Chao Hong, Xi Wang, Jinli Shi, Tian Yuan, Jian Zhou, Yina Cun
article en
2 citations

Abstract

N-glycosylation of rabies virus glycoprotein dynamically regulates protein folding, stability, and antigenicity. Therefore, regulation of N-glycan modification is key to improving vaccine stability and protective efficacy. How the type and modification sites of N-glycans affect the protective efficacy of rabies vaccines remains unclear. Our research indicates that there are differences in the protective efficacy of rabies virus G-proteins modified with different N-glycans. Moreover, the modification of the three-branched hybrid glycan at the aa 319 site of G-protein significantly altered the hydrophobicity, flexibility, and radius, and increased its trimeric antigen instability through molecular dynamics demonstrations. These findings update the current understanding of the impact of glycans on vaccine antigenicity and develop a system to evaluate the stability of antigen glycoproteins based on molecular dynamics.

Journal of VirologyVol. 99(3)
Chinese Academy of Medical Sciences & Peking Union Medical College (CN), National Medical Products Administration (CN), National Institutes for Food and Drug Control (CN), Institute of Medical Biology (SG)
Good health and well-being
Openalex Percentile: Top 16%
Rabies epidemiology and control
2.07
DOIOpen Access PDFOpenAlex
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