ArticleJournal of virology2024
Novel virulence determinants in VP1 regulate the assembly of enterovirus-A71.
Article in Journal of virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Complete genome sequencing and molecular characterization of indigenous enterovirus A71 genogroups D and G of India.Virology journal · 2026Article
- Advances in Antiviral Drug Development Targeting Enteroviruses: From Viral Proteins to Host Factors.Viruses · 2026Review
- Mutation of the highly conserved amino acids in the N-terminal region of the EV-A71 VP1 protein impairs viral RNA release during virus entry.Microbiology spectrum · 2026Article
- Review
- A CRISPR/Cas12a-based reverse transcription multiple cross displacement amplification technique for sensitive, rapid, and highly specific detection ofFrontiers in microbiology · 2026Article
- Serial passagingFrontiers in cellular and infection microbiology · 2026Article
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Authors and funding
18 authors.
Funding
Abstract
Enterovirus-A71 (EV-A71) is the second most common causative agent after coxsackievirus A16 of hand, foot, and mouth disease. The capsids of EV-A71 consist of 60 copies of each of the four viral structural proteins (VP1-VP4). VP1 is highly exposed and surface accessible, playing a central role in virus particle assembly, attachment, and entry. To gain insight into the role of highly conserved residues at positions 75, 78, and 88 in the capsid protein VP1 in these processes, an alanine-scanning analysis was performed using an infectious cDNA clone of EV-A71. Our study revealed that the substitutions of VP1-T75A, VP1-T78A, and VP1-G88A could affect the assembly of the virus capsid proteins, resulting in the production of abnormal virions with reduced infectivity. Specifically, the substitution of VP1-T75A affected the maturation cleavage of the VP0 precursor, leading to deficiencies in binding to receptor scavenger receptor class B2 (SCARB2), viral attachment, internalization, and even uncoating. For the mutants of T78A and G88A, a significant reduction in virion-associated genomic RNA was observed, suggesting that more noninfectious empty particles were produced during viral assembly. Interestingly, the VP1-T75A variant showed weak replication in cell cultures but demonstrated increased virulence in BALB/c neonatal mice, which might be due to the difference in viral receptors among mammalian species. Taken together, our data revealed the important role of the highly conserved residues T75, T78, and G88 in VP1 protein in the infectivity of EV-A71. Characterizing these novel determinants of EV-A71 virulence would contribute to rationally developing effective treatments and broadly protective vaccine candidates. IMPORTANCE: EV-A71 causes hand, foot, and mouth disease in children. In this study, we discovered three highly conserved residues at positions 75, 78, and 88 of the capsid protein VP1 as the potential virulence determinants of EV-A71, which can influence viral replication by regulating the assembly of EV-A71. Mechanistic studies revealed that VP1-T75A could affect the maturation cleavage of the VP0 precursor, resulting in deficiencies in binding to the receptor SCARB2, viral attachment, internalization, and even uncoating. For the mutants of T78A and G88A, more noninfectious empty particles were produced during viral assembly. The discovery of these novel determinants of EV-A71 virulence will promote the study of the pathogenesis of enteroviruses.
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