J 2022

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

BÜTTNER, Carina Renate; Radovan SPURNÝ; Tibor FÜZIK and Pavel PLEVKA

Basic information

Original name

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

Authors

BÜTTNER, Carina Renate; Radovan SPURNÝ; Tibor FÜZIK and Pavel PLEVKA

Edition

Communications Biology, BERLIN, Nature Research, 2022, 2399-3642

Other information

Language

English

Type of outcome

Article in a journal

Country of publisher

Germany

Confidentiality degree

is not subject to a state or trade secret

References:

URL

Marked to be transferred to RIV

Yes

RIV identification code

RIV/00216224:14740/22:00127051

Organization

Středoevropský technologický institut – Repository – Repository

DOI

https://doi.org/10.1038/s42003-022-03863-2

UT WoS

000849250300006

EID Scopus

2-s2.0-85137153447

Keywords in English

cryoelectron microscopy; Enterovirus; genetics; hand foot and mouth disease; human; virion

Links

GX19-25982X, research and development project. LX22NPO5103, research and development project. CIISB II, large research infrastructures. Czech-BioImaging II, large research infrastructures.
Changed: 19/10/2024 00:50, RNDr. Daniel Jakubík

Abstract

In the original language

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.
Displayed: 2/5/2026 20:34