Time-Dependent Transformation of the Herpesvirus Tegument
Open Access
- 15 August 2009
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 83 (16), 8082-8089
- https://doi.org/10.1128/jvi.00777-09
Abstract
All herpesviruses have a layer of protein called the tegument that lies between the virion membrane and the capsid. The tegument consists of multiple, virus-encoded protein species that together can account for nearly half the total virus protein. To clarify the structure of the tegument and its attachment to the capsid, we used electron microscopy and protein analysis to examine the tegument of herpes simplex virus type 1 (HSV-1). Electron microscopic examination of intact virions revealed that whereas the tegument was asymmetrically distributed around the capsid in extracellular virions, it was symmetrically arranged in cell-associated virus. Examination of virions after treatment with nonionic detergent demonstrated that: (i) in extracellular virus the tegument was resistant to removal with Triton X-100 (TX-100), whereas it was lost nearly completely when cell-associated virus was treated in the same way; (ii) the tegument in TX-100-treated extracellular virions was asymmetrically distributed around the capsid as it is in unextracted virus; and (iii) in some images, tegument was seen to be linked to the capsid by short, regularly spaced connectors. Further analysis was carried out with extracellular virus harvested from cells at different times after infection. It was observed that while the amount of tegument present in virions was not affected by time of harvest, the amount remaining after TX-100 treatment increased markedly as the time of harvest was increased from 24 h to 64 h postinfection. The results support the view that HSV-1 virions undergo a time-dependent change in which the tegument is transformed from a state in which it is symmetrically organized around the capsid and extractable with TX-100 to a state where it is asymmetrically arranged and resistant to extraction.Keywords
This publication has 40 references indexed in Scilit:
- Analysis of the Interaction between the UL11 and UL16 Tegument Proteins of Herpes Simplex VirusJournal of Virology, 2008
- Structural Rearrangement within an Enveloped Virus upon Binding to the Host CellJournal of Virology, 2008
- Comprehensive Characterization of Extracellular Herpes Simplex Virus Type 1 VirionsJournal of Virology, 2008
- Native 3D intermediates of membrane fusion in herpes simplex virus 1 entryProceedings of the National Academy of Sciences of the United States of America, 2008
- Proteolytic Cleavage of VP1-2 Is Required for Release of Herpes Simplex Virus 1 DNA into the NucleusJournal of Virology, 2008
- Dynamic Interactions of the UL16 Tegument Protein with the Capsid of Herpes Simplex VirusJournal of Virology, 2007
- Uncoating the Herpes Simplex Virus GenomeJournal of Molecular Biology, 2007
- Interaction of herpes simplex virus RNase with VP16 and VP22 is required for the accumulation of the protein but not for accumulation of mRNAProceedings of the National Academy of Sciences of the United States of America, 2007
- Allosteric Signaling and a Nuclear Exit Strategy: Binding of UL25/UL17 Heterodimers to DNA-Filled HSV-1 CapsidsMolecular Cell, 2007
- The Amino Terminus of the Herpes Simplex Virus 1 Protein Vhs Mediates Membrane Association and Tegument IncorporationJournal of Virology, 2006