Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating

Ling Zhu (), Yao Sun, Jinyan Fan, Bin Zhu, Lei Cao, Qiang Gao, Yanjun Zhang (), Hongrong Liu, Zihe Rao () and Xiangxi Wang ()
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Ling Zhu: Chinese Academy of Sciences
Yao Sun: Chinese Academy of Sciences
Jinyan Fan: Major Project Department
Bin Zhu: Hunan Normal University
Lei Cao: Chinese Academy of Sciences
Qiang Gao: Sinovac Biotech Co., Ltd
Yanjun Zhang: Zhejiang Provincial Center for Disease Control and Prevention
Hongrong Liu: Hunan Normal University
Zihe Rao: Chinese Academy of Sciences
Xiangxi Wang: Chinese Academy of Sciences

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: Abstract Coxsackievirus A10 (CVA10), a human type-A Enterovirus (HEV-A), can cause diseases ranging from hand-foot-and-mouth disease to polio-myelitis-like disease. CVA10, together with some other HEV-As, utilizing the molecule KREMEN1 as an entry receptor, constitutes a KREMEN1-dependent subgroup within HEV-As. Currently, there is no vaccine or antiviral therapy available for treating diseases caused by CVA10. The atomic-resolution structure of the CVA10 virion, which is within the KREMEN1-dependent subgroup, shows significant conformational differences in the putative receptor binding sites and serotype-specific epitopes, when compared to the SCARB2-dependent subgroup of HEV-A, such as EV71, highlighting specific differences between the sub-groups. We also report two expanded structures of CVA10, an empty particle and uncoating intermediate at atomic resolution, as well as a medium-resolution genome structure reconstructed using a symmetry-mismatch method. Structural comparisons coupled with previous results, reveal an ordered signal transmission process for enterovirus uncoating, converting exo-genetic receptor-attachment inputs into a generic RNA release mechanism.

Date: 2018
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DOI: 10.1038/s41467-018-07531-0

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