Journal
JOURNAL OF VIROLOGY
Volume 78, Issue 17, Pages 9560-9563Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.78.17.9560-9563.2004
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Funding
- NIAID NIH HHS [R01AI50111, R01 AI050111] Funding Source: Medline
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Human immunodeficiency virus type 1 (HIV-1) Gag multimerization and membrane binding are required for particle formation. However, it is unclear what constitutes a minimal plasma membrane-specific targeting signal and what role the matrix (MA) globular head and other Gag domains play in membrane targeting. Here, we use membrane flotation and microscopic analysis of Gag deletion mutants to demonstrate that the HIV-1 MA globular head inhibits a plasma membrane-specific targeting signal contained within the six amino-terminal MA residues. MA-mediated inhibition is relieved by concentration-dependent Gag multimerization and imparts a high degree of cooperativity on Gag-membrane association. This cooperativity may confer temporal and spatial regulation on HIV-1 assembly.
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