Atomic structure of the Epstein-Barr virus portal

Cristina Machón, Montserrat Fàbrega-Ferrer, Daming Zhou, Ana Cuervo, José L. Carrascosa, David I. Stuart and Miquel Coll ()
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Cristina Machón: The Barcelona Institute of Science and Technology (BIST)
Montserrat Fàbrega-Ferrer: The Barcelona Institute of Science and Technology (BIST)
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)

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-11706-8

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