Journal
JOURNAL OF VIROLOGY
Volume 77, Issue 3, Pages 2038-2045Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.77.3.2038-2045.2003
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Funding
- NCI NIH HHS [R01 CA080723, P30 CA013330, P30-CA13330, CA80723] Funding Source: Medline
- NIAID NIH HHS [R01 AI038265, AI38265] Funding Source: Medline
- NIGMS NIH HHS [T32 GM007491, T32 GM07491] Funding Source: Medline
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Virion host shutoff (vhs) is a 58-kDa protein encoded by the UL41 gene of herpes simplex virus (HSV). vhs resides within the tegument of HSV, enters the cell cytoplasm at infection, and destabilizes host cell and viral mRNA. Late in infection, vhs must be assembled into the tegument of progeny virions, a poorly understood process. Using an anti-vhs antiserum and Western blotting of total cell or cytoplasmic extracts, we found that vhs is largely insoluble in HSV-infected cells, even in the presence of high levels of salt and the detergent Triton X-100. Furthermore, a subpopulation of vhs appears to be associated with detergent-insoluble lipid rafts and this raft population is enriched in a cytoplasmic fraction which contains assembling and mature HSV particles. Our data raise the possibility that HSV tegument polypeptides associate with membrane rafts, in common with the matrix proteins of a number of other viruses.
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