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 language | English (US) |
---|---|
Pages (from-to) | 89-102 |
Number of pages | 14 |
Journal | Virology |
Volume | 408 |
Issue number | 1 |
DOIs | |
State | Published - Dec 5 2010 |
Keywords
- CD4 down-regulation
- HIV-1
- Lipid rafts
- Membrane rafts
- Virus release
- Vpu
ASJC Scopus subject areas
- Virology