Atomic structure of the Epstein-Barr virus portal

• Published in: Nature communications 2019-08, Vol.10 (1), p.3891-7, Article 3891
• Main Authors: Machón, Cristina, Fàbrega-Ferrer, Montserrat, Zhou, Daming, Cuervo, Ana, Carrascosa, José L., Stuart, David I., Coll, Miquel
• Format: Article
• Language: English
• Subjects: 101/28; 631/326/596/1553; 631/535/1258/1259; Antiviral agents; Atomic structure; Capsid - ultrastructure; Capsid Proteins - genetics; Capsid Proteins - ultrastructure; Cryoelectron Microscopy; Deoxyribonucleic acid; DNA; DNA Packaging; DNA viruses; DNA, Viral - genetics; Electron microscopy; Entrances; Epithelial cells; Epstein-Barr virus; Genome, Viral; Genomes; Herpesvirus 4, Human - genetics; Herpesvirus 4, Human - ultrastructure; Human behavior; Humanities and Social Sciences; Humans; Icosahedral phase; Infectious mononucleosis; Lymphocytes B; Models, Molecular; Mononucleosis; multidisciplinary; Packaging; Portal protein; Protein Conformation; Protein Interaction Domains and Motifs; Protein structure; Proteins; Science; Science (multidisciplinary); Vaccines; Viral Envelope Proteins - genetics; Viral Envelope Proteins - ultrastructure; Viral Proteins - genetics; Viral Proteins - ultrastructure; Virion - ultrastructure; Virus Assembly; Viruses
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-019-11706-8

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. The Epstein-Barr virus (EBV) is a dangerous human pathogen responsible for mononucleosis and several types of cancers. Here the authors describe a high-resolution atomic structure of the EBV portal, which serves as the entrance and exit pore for the viral genome and is a potential pharmacological target for the development of antivirals.