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Nat Commun. 2019 Aug 29;10(1):3891. doi: 10.1038/s41467-019-11706-8.

Atomic structure of the Epstein-Barr virus portal.

Author information

1
Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10-12, 08028, Barcelona, Spain.
2
Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, 08028, Barcelona, Spain.
3
Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford, OX3 7BN, UK.
4
Department of Macromolecular Structures, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), 28049, Madrid, Spain.
5
Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10-12, 08028, Barcelona, Spain. miquel.coll@irbbarcelona.org.
6
Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri Reixac 10-12, 08028, Barcelona, Spain. miquel.coll@irbbarcelona.org.

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.

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