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Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion

Author

Listed:
  • Na Zhang

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
    Graduate University, Chinese Academy of Sciences)

  • Jinghua Yan

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences)

  • Guangwen Lu

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences)

  • Zhengfei Guo

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
    School of Life Sciences, Anhui University)

  • Zheng Fan

    (Core Facility, Institute of Microbiology, Chinese Academy of Sciences)

  • Jiawei Wang

    (State Key Laboratory of Biomembrane, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University)

  • Yi Shi

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences)

  • Jianxun Qi

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences)

  • George F Gao

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
    Graduate University, Chinese Academy of Sciences
    Research Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences)

Abstract

Multiple surface envelope proteins are involved in the human herpes simplex virus type 1 entry and fusion. Among them, glycoprotein D (gD) has an important role by binding to the host receptors such as herpes virus entry mediator and nectin-1. Although the complex structure of gD with herpes virus entry mediator has been established, the binding mode of gD with the nectin-1 is elusive. Nectin-1 is a member of the immunoglobulin (Ig)-like (three Ig-like domains) cell adhesion molecules and is believed to form a homodimer to exert its functions. Here we report the complex structure of gD and nectin-1 (three Ig domains), revealing that gD binds the first Ig domain of nectin-1 in a similar mode to the nectin-1 homodimer interaction. The key amino acids responsible for nectin-1 dimerization are also used for gD/nectin-1 binding. This result indicates that binding of gD to nectin-1 would preclude the nectin-1 dimerization, consequently abolishing its cell adhesion function.

Suggested Citation

  • Na Zhang & Jinghua Yan & Guangwen Lu & Zhengfei Guo & Zheng Fan & Jiawei Wang & Yi Shi & Jianxun Qi & George F Gao, 2011. "Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion," Nature Communications, Nature, vol. 2(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1571
    DOI: 10.1038/ncomms1571
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