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TitleConformational Flexibility in Capsids Encoded by the .
Journal, issue, pagesViruses, Vol. 16, Issue 12, Year 2024
Publish dateNov 26, 2024
AuthorsCharlotte B Lewis / Lee Sherry / Michaela J Conley / Masaaki Nakashima / Shirin Akbar / Nithya Govindan / Margaret J Hosie / David Bhella /
PubMed AbstractCaliciviruses are a diverse group of non-enveloped, positive-sense RNA viruses with a wide range of hosts and transmission routes. Norovirus is the most well-known member of the ; the acute ...Caliciviruses are a diverse group of non-enveloped, positive-sense RNA viruses with a wide range of hosts and transmission routes. Norovirus is the most well-known member of the ; the acute gastroenteritis caused by human norovirus (HuNoV), for example, frequently results in closures of hospital wards and schools during the winter months. One area of calicivirus biology that has gained increasing attention over the past decade is the conformational flexibility exhibited by the protruding (P) domains of the major capsid protein VP1. This was observed in structure analyses of capsids encoded by many species and is often a consequence of environmental cues such as metal ions, changes to pH, or receptor/co-factor engagement. This review summarises the current understanding of P-domain flexibility, discussing the role this region plays in caliciviral infection and immune evasion, and highlighting potential avenues for further investigation.
External linksViruses / PubMed:39772145 / PubMed Central
MethodsEM (single particle)
Resolution2.6 Å
Structure data

52037

9hc5

EMDB-52037, PDB-9hc5:
Structure of Tulane virus
Method: EM (single particle) / Resolution: 2.6 Å

Source
  • tulane virus
KeywordsVIRUS / Capsid / Tulane Virus / Calicivirus

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