Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00127051" target="_blank" >RIV/00216224:14740/22:00127051 - isvavai.cz</a>

Result on the web

<a href="https://www.nature.com/articles/s42003-022-03863-2" target="_blank" >https://www.nature.com/articles/s42003-022-03863-2</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s42003-022-03863-2" target="_blank" >10.1038/s42003-022-03863-2</a>

Result language

angličtina

Original language name

Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion

Original language description

Coxsackievirus A6 (CV-A6) has recently overtaken enterovirus A71 and CV-A16 as the primary causative agent of hand, foot, and mouth disease worldwide. Virions of CV-A6 were not identified in previous structural studies, and it was speculated that the virus is unique among enteroviruses in using altered particles with expanded capsids to infect cells. In contrast, the virions of other enteroviruses are required for infection. Here we used cryo-electron microscopy (cryo-EM) to determine the structures of the CV-A6 virion, altered particle, and empty capsid. We show that the CV-A6 virion has features characteristic of virions of other enteroviruses, including a compact capsid, VP4 attached to the inner capsid surface, and fatty acid-like molecules occupying the hydrophobic pockets in VP1 subunits. Furthermore, we found that in a purified sample of CV-A6, the ratio of infectious units to virions is 1 to 500. Therefore, it is likely that virions of CV-A6 initiate infection, like those of other enteroviruses. Our results provide evidence that future vaccines against CV-A6 should target its virions instead of the antigenically distinct altered particles. Furthermore, the structure of the virion provides the basis for the rational development of capsid-binding inhibitors that block the genome release of CV-A6. A cryo-EM structure for the three conformers of coxsackievirus A6 provides insight into the infection process of this enterovirus, which is responsible for numerous cases of hand, foot, and mouth disease.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10607 - Virology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Communications Biology

ISSN

2399-3642

e-ISSN

—

Volume of the periodical

5

Issue of the periodical within the volume

1

Country of publishing house

DE - GERMANY

Number of pages

10

Pages from-to

898

UT code for WoS article

000849250300006

EID of the result in the Scopus database

2-s2.0-85137153447