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

Author

Listed:
  • Yuguang Zhao

    (University of Oxford)

  • Daming Zhou

    (University of Oxford)

  • Tao Ni

    (University of Oxford)

  • Dimple Karia

    (University of Oxford)

  • Abhay Kotecha

    (University of Oxford
    Thermo Fisher Scientific)

  • Xiangxi Wang

    (Chinese Academy of Science)

  • Zihe Rao

    (Chinese Academy of Science)

  • E. Yvonne Jones

    (University of Oxford)

  • Elizabeth E. Fry

    (University of Oxford)

  • Jingshan Ren

    (University of Oxford)

  • David I. Stuart

    (University of Oxford
    Diamond Light Source Ltd)

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.

Suggested Citation

  • 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, 2020. "Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10," Nature Communications, Nature, vol. 11(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-019-13936-2
    DOI: 10.1038/s41467-019-13936-2
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    Cited by:

    1. Chao Zhang & Caixuan Liu & Jinping Shi & Yalei Wang & Cong Xu & Xiaohua Ye & Qingwei Liu & Xue Li & Weihua Qiao & Yannan Yin & Yao Cong & Zhong Huang, 2022. "Molecular mechanism of antibody neutralization of coxsackievirus A16," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Ruth E. Drury & Susana Camara & Irina Chelysheva & Sagida Bibi & Katherine Sanders & Salle Felle & Katherine Emary & Daniel Phillips & Merryn Voysey & Daniela M. Ferreira & Paul Klenerman & Sarah C. G, 2024. "Multi-omics analysis reveals COVID-19 vaccine induced attenuation of inflammatory responses during breakthrough disease," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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