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5XS7

Structure of Coxsackievirus A6 (CVA6) virus A-particle in complex with the neutralizing antibody fragment 1D5

Summary for 5XS7
Entry DOI10.2210/pdb5xs7/pdb
EMDB information6757
DescriptorLight chain of Fab 1D5, Heavy chain of Fab 1D5, Genome polyprotein, ... (5 entities in total)
Functional Keywordscoxsackievirus a6, immune-complex, icosahedral, virus
Biological sourceMus musculus
More
Cellular locationHost cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : A0A0K2BNC7 A0A0K2BNC7 A0A0K2BNC7
Total number of polymer chains5
Total formula weight112975.76
Authors
Zheng, Q.B.,He, M.Z.,Xu, L.F.,Yu, H.,Li, S.W.,Cheng, T. (deposition date: 2017-06-12, release date: 2017-09-27, Last modification date: 2024-10-30)
Primary citationXu, L.,Zheng, Q.,Li, S.,He, M.,Wu, Y.,Li, Y.,Zhu, R.,Yu, H.,Hong, Q.,Jiang, J.,Li, Z.,Li, S.,Zhao, H.,Yang, L.,Hou, W.,Wang, W.,Ye, X.,Zhang, J.,Baker, T.S.,Cheng, T.,Zhou, Z.H.,Yan, X.,Xia, N.
Atomic structures of Coxsackievirus A6 and its complex with a neutralizing antibody
Nat Commun, 8:505-505, 2017
Cited by
PubMed Abstract: Coxsackievirus A6 (CVA6) has recently emerged as a major cause of hand, foot and mouth disease in children worldwide but no vaccine is available against CVA6 infections. Here, we demonstrate the isolation of two forms of stable CVA6 particles-procapsid and A-particle-with excellent biochemical stability and natural antigenicity to serve as vaccine candidates. Despite the presence (in A-particle) or absence (in procapsid) of capsid-RNA interactions, the two CVA6 particles have essentially identical atomic capsid structures resembling the uncoating intermediates of other enteroviruses. Our near-atomic resolution structure of CVA6 A-particle complexed with a neutralizing antibody maps an immune-dominant neutralizing epitope to the surface loops of VP1. The structure-guided cell-based inhibition studies further demonstrate that these loops could serve as excellent targets for designing anti-CVA6 vaccines.Coxsackievirus A6 (CVA6) causes hand, foot and mouth disease in children. Here the authors present the CVA6 procapsid and A-particle cryo-EM structures and identify an immune-dominant neutralizing epitope, which can be exploited for vaccine development.
PubMed: 28894095
DOI: 10.1038/s41467-017-00477-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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