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.
Highlights
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 lifethreatening
The structure was solved by symmetry relaxation of the whole virion, with the portal determined at 5.6 Å resolution, coordinates and maps were not yet available for precise comparison with our Epstein-Barr virus (EBV) portal[19]
The quality and homogeneity of the sample was tested by negative-stain electron microscopy and purified protein was used for single-particle cryo-EM (Supplementary Fig. 1), and two different datasets were collected from different preparations
Summary
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 lifethreatening. The structure determination at high resolution of portal proteins from bacteriophages has been successful with examples of gp[6] from SPP1, gp[1] from P22, gp[20] from T4, and gp[10] from φ29, solved by X-ray crystallography and cryo-EM10–14. We present the atomic structure of the EBV portal solved by cryo-electron microscopy at 3.5 Å resolution, showing its detailed architectural features.
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