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Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10

DOI: 10.1038/s41467-019-13936-2 DOI Help

Authors: Yuguang Zhao (The Wellcome Centre for Human Genetics, University of Oxford) , Daming Zhou (The Wellcome Centre for Human Genetics, University of Oxford) , Tao Ni (The Wellcome Centre for Human Genetics, University of Oxford) , Dimple Karia (The Wellcome Centre for Human Genetics, University of Oxford) , Abhay Kotecha (The Wellcome Centre for Human Genetics, University of Oxford; Thermo Fisher Scientific) , Xiangxi Wang (Institute of Biophysics, Chinese Academy of Science) , Zihe Rao (Institute of Biophysics, Chinese Academy of Science) , E. Yvonne Jones (The Wellcome Centre for Human Genetics, University of Oxford) , Elizabeth E. Fry (University of Oxford) , Jingshan Ren (The Wellcome Centre for Human Genetics, University of Oxford) , David I. Stuart (The Wellcome Centre for Human Genetics, University of Oxford; Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 11

State: Published (Approved)
Published: January 2020

Open Access Open Access

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.

Journal Keywords: Cryoelectron microscopy; Viral infection; Virus structures

Subject Areas: Biology and Bio-materials


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s41467-019-13936-2.pdf