Membrane raft association of the Vpu protein of human immunodeficiency virus type 1 correlates with enhanced virus release

Autumn Ruiz, M. Sarah Hill, Kimberly Schmitt, Edward B. Stephens

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

The Vpu protein of human immunodeficiency virus type 1 (HIV-1) is known to enhance virion release from certain cell types. To accomplish this function, Vpu interacts with the restriction factor known as bone marrow stromal cell antigen 2 (BST-2)/tetherin. In this study, we analyzed whether the Vpu protein is associated with microdomains known as lipid or membrane rafts. Our results indicate that Vpu partially partitions into detergent-resistant membrane (DRM) fractions when expressed alone or in the context of simian-human immunodeficiency virus (SHIV) infection. The ability to be partitioned into rafts was observed with both subtype B and C Vpu proteins. The use of cholesterol lowering lovastatin/M-β-cyclodextrin and co-patching experiments confirmed that Vpu can be detected in cholesterol rich regions of membranes. Finally, we present data showing that raft association-defective transmembrane mutants of Vpu have impaired enhanced virus release function, but still maintain the ability to down-regulate CD4.

Original languageEnglish (US)
Pages (from-to)89-102
Number of pages14
JournalVirology
Volume408
Issue number1
DOIs
StatePublished - Dec 5 2010

Keywords

  • CD4 down-regulation
  • HIV-1
  • Lipid rafts
  • Membrane rafts
  • Virus release
  • Vpu

ASJC Scopus subject areas

  • Virology

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