Herpes Simplex Virus Capsid-Organelle Association in the Absence of the Large Tegument Protein UL36p

Journal of Virology
Himanshu KharkwalDuncan W Wilson

Abstract

UL36p (VP1/2) is the largest protein encoded by herpes simplex virus 1 (HSV-1) and resides in the innermost layer of the viral tegument, lying between the capsid and the envelope. UL36p performs multiple functions in the HSV life cycle, including an essential role in cytoplasmic envelopment. We earlier described the isolation of a virion-associated cytoplasmic membrane fraction from HSV-infected cells. Biochemical and ultrastructural analyses showed that the organelles in this buoyant fraction contain enveloped infectious HSV particles in their lumens and naked capsids docked to their cytoplasmic surfaces. These organelles can also recruit molecular motors and transport their cargo virions along microtubules in vitro. Here we examine the properties of these HSV-associated organelles in the absence of UL36p. We find that while capsid envelopment is clearly defective, a subpopulation of capsids nevertheless still associate with the cytoplasmic faces of these organelles. The existence of these capsid-membrane structures was confirmed by subcellular fractionation, immunocytochemistry, lipophilic dye fluorescence microscopy, thin-section electron microscopy, and correlative light and electron microscopy. We conclude that capsid-memb...Continue Reading

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Citations

Feb 15, 2017·Journal of Peptide Science : an Official Publication of the European Peptide Society·Gianluigi FranciMassimiliano Galdiero
Apr 19, 2019·Journal of Virology·Jenna Barnes, Duncan W Wilson
Aug 23, 2020·International Journal of Molecular Sciences·Imran Ahmad, Duncan W Wilson
Sep 1, 2021·Current Opinion in Virology·Katinka DöhnerBeate Sodeik

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