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Atomic structure of the human herpesvirus 6B capsid and capsid-associated tegument complexes

Author

Listed:
  • Yibo Zhang

    (University of Science and Technology of China (USTC)
    University of California, Los Angeles (UCLA))

  • Wei Liu

    (University of Science and Technology of China (USTC)
    University of California, Los Angeles (UCLA)
    Immunology and Molecular Genetics, UCLA
    East China Normal University (ECNU))

  • Zihang Li

    (University of California, Los Angeles (UCLA)
    Immunology and Molecular Genetics, UCLA)

  • Vinay Kumar

    (University of California, Los Angeles (UCLA)
    Immunology and Molecular Genetics, UCLA)

  • Ana L. Alvarez-Cabrera

    (University of California, Los Angeles (UCLA)
    Immunology and Molecular Genetics, UCLA)

  • Emily C. Leibovitch

    (National Institutes of Health (NIH))

  • Yanxiang Cui

    (University of California, Los Angeles (UCLA))

  • Ye Mei

    (East China Normal University (ECNU))

  • Guo-Qiang Bi

    (University of Science and Technology of China (USTC))

  • Steve Jacobson

    (National Institutes of Health (NIH))

  • Z. Hong Zhou

    (University of California, Los Angeles (UCLA)
    Immunology and Molecular Genetics, UCLA)

Abstract

Human herpesvirus 6B (HHV-6B) belongs to the β-herpesvirus subfamily of the Herpesviridae. To understand capsid assembly and capsid-tegument interactions, here we report atomic structures of HHV-6B capsid and capsid-associated tegument complex (CATC) obtained by cryoEM and sub-particle reconstruction. Compared to other β-herpesviruses, HHV-6B exhibits high similarity in capsid structure but organizational differences in its CATC (pU11 tetramer). 180 “VΛ”-shaped CATCs are observed in HHV-6B, distinguishing from the 255 “Λ”-shaped dimeric CATCs observed in murine cytomegalovirus and the 310 “Δ”-shaped CATCs in human cytomegalovirus. This trend in CATC quantity correlates with the increasing genomes sizes of these β-herpesviruses. Incompatible distances revealed by the atomic structures rationalize the lack of CATC’s binding to triplexes Ta, Tc, and Tf in HHV-6B. Our results offer insights into HHV-6B capsid assembly and the roles of its tegument proteins, including not only the β-herpesvirus-specific pU11 and pU14, but also those conserved across all subfamilies of Herpesviridae.

Suggested Citation

  • Yibo Zhang & Wei Liu & Zihang Li & Vinay Kumar & Ana L. Alvarez-Cabrera & Emily C. Leibovitch & Yanxiang Cui & Ye Mei & Guo-Qiang Bi & Steve Jacobson & Z. Hong Zhou, 2019. "Atomic structure of the human herpesvirus 6B capsid and capsid-associated tegument complexes," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13064-x
    DOI: 10.1038/s41467-019-13064-x
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    Cited by:

    1. Guosong Wang & Zhenghui Zha & Pengfei Huang & Hui Sun & Yang Huang & Maozhou He & Tian Chen & Lina Lin & Zhenqin Chen & Zhibo Kong & Yuqiong Que & Tingting Li & Ying Gu & Hai Yu & Jun Zhang & Qingbing, 2022. "Structures of pseudorabies virus capsids," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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