Sequences in the UL11 tegument protein of herpes simplex virus that control association with detergent-resistant membranes

Abstract The product of the UL 11 gene of HSV-1 is a small, membrane-bound tegument protein with features that are conserved among all herpesviruses. For all viruses examined, mutants lacking this protein (or its homolog) have budding defects and accumulate capsids in the cytoplasm of the infected c...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2008-05, Vol.374 (2), p.315-321
Main Authors: Baird, Nicholas L, Yeh, Pei-Chun, Courtney, Richard J, Wills, John W
Format: Article
Language:English
Subjects:
Acidic cluster
Animals
Cell Line, Tumor
Cell Membrane - chemistry
Cell Membrane - drug effects
Cell Membrane - metabolism
Cercopithecus aethiops
Detergents - pharmacology
Di-leucine
DRM
Gene Expression Regulation, Viral
Herpes simplex
Herpes simplex virus 1
Herpesvirus 1, Human - genetics
Herpesvirus 1, Human - metabolism
Herpesvirus 1, Human - pathogenicity
Humans
Infectious Disease
Lipid raft
Myristate
Myristates - metabolism
Octoxynol - pharmacology
Palmitate
Palmitates - metabolism
UL11
Vero Cells
Viral Structural Proteins - chemistry
Viral Structural Proteins - genetics
Viral Structural Proteins - metabolism
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Summary:Abstract The product of the UL 11 gene of HSV-1 is a small, membrane-bound tegument protein with features that are conserved among all herpesviruses. For all viruses examined, mutants lacking this protein (or its homolog) have budding defects and accumulate capsids in the cytoplasm of the infected cell. UL11 binds to the cytoplasmic faces of host membranes via N-terminal myristate and nearby palmitate moieties. These fatty-acid modifications are typical of proteins that localize to detergent-resistant membranes (DRMs), and the experiments described here revealed that a small amount (∼ 10%) of UL11 retains the ability to float in sucrose gradients following treatment of cells with Triton X-100. However, mutants lacking sequences previously shown to be involved in the trafficking of UL11 from the plasma membrane (LI and acidic cluster motifs) were found to have a dramatically increased association with DRMs. These findings emphasize the dynamic properties of this poorly-understood but conserved tegument protein.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2008.01.007