6AKS

Cryo-EM structure of CVA10 mature virus

Summary for 6AKS

• Entry DOI: 10.2210/pdb6aks/pdb
• EMDB information: 9642
• Descriptor: VP1, VP2, VP3, ... (5 entities in total)
• Functional Keywords: picornavirus uncoating, receptor binding, virus
• Biological source: Coxsackievirus A10; More
• Total number of polymer chains: 4
• Total formula weight: 94927.72

Authors

Zhu, L.,Sun, Y.,Fan, J.Y.,Zhu, B.,Cao, L.,Gao, Q.,Zhang, Y.J.,Liu, H.R.,Rao, Z.H.,Wang, X.X. (deposition date: 2018-09-03, release date: 2019-01-16, Last modification date: 2024-03-27)

Primary citation

Zhu, L.,Sun, Y.,Fan, J.,Zhu, B.,Cao, L.,Gao, Q.,Zhang, Y.,Liu, H.,Rao, Z.,Wang, X.
Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating.
Nat Commun, 9:4985-4985, 2018

PubMed 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.

PubMed: 30478256
DOI: 10.1038/s41467-018-07531-0

Experimental method

ELECTRON MICROSCOPY (3 Å)