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TitleCryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.
Journal, issue, pagesCell Host Microbe, Vol. 29, Issue 3, Page 448-462.e5, Year 2021
Publish dateMar 10, 2021
AuthorsLongfa Xu / Qingbing Zheng / Rui Zhu / Zhichao Yin / Hai Yu / Yu Lin / Yuanyuan Wu / Maozhou He / Yang Huang / Yichao Jiang / Hui Sun / Zhenghui Zha / Hongwei Yang / Qiongzi Huang / Dongqing Zhang / Zhenqin Chen / Xiangzhong Ye / Jinle Han / Lisheng Yang / Che Liu / Yuqiong Que / Mujin Fang / Ying Gu / Jun Zhang / Wenxin Luo / Z Hong Zhou / Shaowei Li / Tong Cheng / Ningshao Xia /
PubMed AbstractEnterovirus uncoating receptors bind at the surface depression ("canyon") that encircles each capsid vertex causing the release of a host-derived lipid called "pocket factor" that is buried in a ...Enterovirus uncoating receptors bind at the surface depression ("canyon") that encircles each capsid vertex causing the release of a host-derived lipid called "pocket factor" that is buried in a hydrophobic pocket formed by the major viral capsid protein, VP1. Coxsackievirus and adenovirus receptor (CAR) is a universal uncoating receptor of group B coxsackieviruses (CVB). Here, we present five high-resolution cryoEM structures of CVB representing different stages of virus infection. Structural comparisons show that the CAR penetrates deeper into the canyon than other uncoating receptors, leading to a cascade of events: collapse of the VP1 hydrophobic pocket, high-efficiency release of the pocket factor and viral uncoating and genome release under neutral pH, as compared with low pH. Furthermore, we identified a potent therapeutic antibody that can neutralize viral infection by interfering with virion-CAR interactions, destabilizing the capsid and inducing virion disruption. Together, these results define the structural basis of CVB cell entry and antibody neutralization.
External linksCell Host Microbe / PubMed:33539764 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.8 Å
Structure data

30805

7dpf

EMDB-30805, PDB-7dpf:
Cryo-EM structure of Coxsackievirus B1 mature virion
Method: EM (single particle) / Resolution: 3.2 Å

30806

7dpg

EMDB-30806, PDB-7dpg:
Cryo-EM structure of Coxsackievirus B1 empty particle
Method: EM (single particle) / Resolution: 3.4 Å

30812

7dpz

EMDB-30812, PDB-7dpz:
Cryo-EM structure of Coxsackievirus B1 virion in complex with CAR
Method: EM (single particle) / Resolution: 3.8 Å

30813

7dq1

EMDB-30813, PDB-7dq1:
Cryo-EM structure of Coxsackievirus B1 virion in complex with CAR at physiological temperature
Method: EM (single particle) / Resolution: 3.6 Å

30814

7dq4

EMDB-30814, PDB-7dq4:
Cryo-EM structure of CAR triggered Coxsackievirus B1 A-particle
Method: EM (single particle) / Resolution: 3.8 Å

30815

7dq7

EMDB-30815, PDB-7dq7:
Cryo-EM structure of Coxsackievirus B1 mature virion in complex with nAb 5F5
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID

Source
  • coxsackievirus b1
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsVIRUS / Coxsackievirus B1 / mature virion / Cryo-EM / empty particle / CAR / A-particle / VIRUS/IMMUNE SYSTEM / neutralizing antibody / VIRUS-IMMUNE SYSTEM complex

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