Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10
Yuguang Zhao, Daming Zhou, Tao Ni, Dimple Karia, Abhay Kotecha, Xiangxi Wang, Zihe Rao, E. Yvonne Jones, Elizabeth E. Fry, Jingshan Ren & David I. Stuart
Abstract
Coxsackievirus A10 (CV-A10) is responsible for an escalating number of severe infections in children, but no prophylactics or therapeutics are currently available. KREMEN1 (KRM1) is the entry receptor for the largest receptor-group of hand-foot-and-mouth disease causing viruses, which includes CV-A10. We report here structures of CV-A10 mature virus alone and in complex with KRM1 as well as of the CV-A10 A-particle. The receptor spans the viral canyon with a large footprint on the virus surface. The footprint has some overlap with that seen for the neonatal Fc receptor complexed with enterovirus E6 but is larger and distinct from that of another enterovirus receptor SCARB2. Reduced occupancy of a particle-stabilising pocket factor in the complexed virus and the presence of both unbound and expanded virus particles suggests receptor binding initiates a cascade of conformational changes that produces expanded particles primed for viral uncoating.
附件下载：
Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10, Nature Comm, 07 Jan 2020
Nature Communications, 07 January, 2020，DOI：http://dx.doi.org/10.1038/s41467-019-13936-2
Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10
Yuguang Zhao, Daming Zhou, Tao Ni, Dimple Karia, Abhay Kotecha, Xiangxi Wang, Zihe Rao, E. Yvonne Jones, Elizabeth E. Fry, Jingshan Ren & David I. Stuart
Abstract
Coxsackievirus A10 (CV-A10) is responsible for an escalating number of severe infections in children, but no prophylactics or therapeutics are currently available. KREMEN1 (KRM1) is the entry receptor for the largest receptor-group of hand-foot-and-mouth disease causing viruses, which includes CV-A10. We report here structures of CV-A10 mature virus alone and in complex with KRM1 as well as of the CV-A10 A-particle. The receptor spans the viral canyon with a large footprint on the virus surface. The footprint has some overlap with that seen for the neonatal Fc receptor complexed with enterovirus E6 but is larger and distinct from that of another enterovirus receptor SCARB2. Reduced occupancy of a particle-stabilising pocket factor in the complexed virus and the presence of both unbound and expanded virus particles suggests receptor binding initiates a cascade of conformational changes that produces expanded particles primed for viral uncoating.
文章链接：http://www-nature-com/articles/s41467-019-13936-2