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Atomic structure of the Epstein-Barr virus portal

Author

Listed:
  • Cristina Machón

    (The Barcelona Institute of Science and Technology (BIST)
    Molecular Biology Institute of Barcelona (IBMB-CSIC))

  • Montserrat Fàbrega-Ferrer

    (The Barcelona Institute of Science and Technology (BIST)
    Molecular Biology Institute of Barcelona (IBMB-CSIC))

  • Daming Zhou

    (University of Oxford)

  • Ana Cuervo

    (Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC))

  • José L. Carrascosa

    (Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC))

  • David I. Stuart

    (University of Oxford)

  • Miquel Coll

    (The Barcelona Institute of Science and Technology (BIST)
    Molecular Biology Institute of Barcelona (IBMB-CSIC))

Abstract

Herpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 Å resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging.

Suggested Citation

  • Cristina Machón & Montserrat Fàbrega-Ferrer & Daming Zhou & Ana Cuervo & José L. Carrascosa & David I. Stuart & Miquel Coll, 2019. "Atomic structure of the Epstein-Barr virus portal," Nature Communications, Nature, vol. 10(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11706-8
    DOI: 10.1038/s41467-019-11706-8
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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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