7C4Y
Cryo-EM structure of empty Coxsackievirus A10 at pH 7.4
Summary for 7C4Y
| Entry DOI | 10.2210/pdb7c4y/pdb |
| EMDB information | 30291 |
| Descriptor | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3 (3 entities in total) |
| Functional Keywords | picornavirus, coxsackievirus a10, ph 7.4, empty particle, virus |
| Biological source | Coxsackievirus A10 More |
| Total number of polymer chains | 3 |
| Total formula weight | 87175.06 |
| Authors | |
| Primary citation | Cui, Y.,Peng, R.,Song, H.,Tong, Z.,Qu, X.,Liu, S.,Zhao, X.,Chai, Y.,Wang, P.,Gao, G.F.,Qi, J. Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1. Proc.Natl.Acad.Sci.USA, 117:18711-18718, 2020 Cited by PubMed Abstract: KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection. PubMed: 32690697DOI: 10.1073/pnas.2005341117 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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