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7VY5

Coxsackievirus B3 (VP3-234Q) incubation with CD55 at pH7.4

Summary for 7VY5
Entry DOI10.2210/pdb7vy5/pdb
EMDB information32194
DescriptorCapsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (6 entities in total)
Functional Keywordscvb3, vp3-234q, cd55, virus
Biological sourceCoxsackievirus B3
More
Total number of polymer chains5
Total formula weight105613.03
Authors
Wang, Q.L.,Liu, C.C. (deposition date: 2021-11-13, release date: 2022-01-19, Last modification date: 2024-10-30)
Primary citationWang, Q.,Yang, Q.,Liu, C.,Wang, G.,Song, H.,Shang, G.,Peng, R.,Qu, X.,Liu, S.,Cui, Y.,Wang, P.,Xu, W.,Zhao, X.,Qi, J.,Yang, M.,Gao, G.F.
Molecular basis of differential receptor usage for naturally occurring CD55-binding and -nonbinding coxsackievirus B3 strains.
Proc.Natl.Acad.Sci.USA, 119:-, 2022
Cited by
PubMed Abstract: Receptor usage defines cell tropism and contributes to cell entry and infection. Coxsackievirus B (CVB) engages coxsackievirus and adenovirus receptor (CAR), and selectively utilizes the decay-accelerating factor (DAF; CD55) to infect cells. However, the differential receptor usage mechanism for CVB remains elusive. This study identified VP3-234 residues (234Q/N/V/D/E) as critical population selection determinants during CVB3 virus evolution, contributing to diverse binding affinities to CD55. Cryoelectron microscopy (cryo-EM) structures of CD55-binding/nonbinding isolates and their complexes with CD55 or CAR were obtained under both neutral and acidic conditions, and the molecular mechanism of VP3-234 residues determining CD55 affinity/specificity for naturally occurring CVB3 strains was elucidated. Structural and biochemical studies in vitro revealed the dynamic entry process of CVB3 and the function of the uncoating receptor CAR with different pH preferences. This work provides detailed insight into the molecular mechanism of CVB infection and contributes to an in-depth understanding of enterovirus attachment receptor usage.
PubMed: 35046043
DOI: 10.1073/pnas.2118590119
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.15 Å)
Structure validation

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