Spanish Ministry of Science, Innovation, and Universities
BFU-2014-53550-P
スペイン
Spanish Ministry of Science, Innovation, and Universities
BFU2017-83720-P
スペイン
Spanish Ministry of Science, Innovation, and Universities
MDM-2014-0435
スペイン
Spanish Ministry of Science, Innovation, and Universities
SEV-2013-0347
スペイン
European Commission
653706
引用
ジャーナル: Nat Commun / 年: 2019 タイトル: Atomic structure of the Epstein-Barr virus portal. 著者: Cristina Machón / Montserrat Fàbrega-Ferrer / Daming Zhou / Ana Cuervo / José L Carrascosa / David I Stuart / Miquel Coll / 要旨: 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. ...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.
A: Portal protein B: Portal protein C: Portal protein D: Portal protein E: Portal protein F: Portal protein G: Portal protein H: Portal protein I: Portal protein J: Portal protein K: Portal protein L: Portal protein