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Atomic structure of the Epstein-Barr virus portal

DOI: 10.1038/s41467-019-11706-8 DOI Help

Authors: Cristina Machon (Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST); Molecular Biology Institute of Barcelona (IBMB-CSIC)) , Montserrat Fàbrega-ferrer (Institute for Research in Biomedicine (IRB Barcelona), 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 (Diamond Light Source) , Miquel Coll (Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST); Molecular Biology Institute of Barcelona (IBMB-CSIC))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: August 2019
Diamond Proposal Number(s): 18360

Open Access Open Access

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.

Journal Keywords: Cryoelectron microscopy; Herpes virus

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond

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s41467-019-11706-8.pdf