Sequences in the UL11 tegument protein of herpes simplex virus that control association with detergent-resistant membranes. Journal   Virology. Citation   Virology. 374(2):315-21 Publication date   2008 May 10 Authors   Baird NL Yeh PC Courtney RJ Wills JW Investigators   Richard J. Courtney John W. Wills Grants   United States NIAID AI071286 United States NCI CA42460 United States NCI CA47482 United States NIAID R01 AI071286-02 United States NCI R01 CA042460-19 United States NCI R37 CA047482-19 MeSH headings   Cell Membrane Detergents Gene Expression Regulation, Viral Octoxynol Viral Structural Proteins MeSH qualifiers   metabolism pharmacology chemistry Abstract   The product of the UL11 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 (approximately 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.