[HTML][HTML] AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding

B Strack, A Calistri, S Craig, E Popova, HG Göttlinger - Cell, 2003 - cell.com
B Strack, A Calistri, S Craig, E Popova, HG Göttlinger
Cell, 2003cell.com
HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a
process requiring membrane fission. The primary late assembly (L) domain in the p6 region
of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component
of the class E vacuolar protein sorting (Vps) machinery. We now show that HIV Gag p6
contains a second region involved in L domain function that binds AIP1, a homolog of the
yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a …
Abstract
HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a process requiring membrane fission. The primary late assembly (L) domain in the p6 region of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component of the class E vacuolar protein sorting (Vps) machinery. We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a subunit of the yeast class E Vps protein complex ESCRT-III. AIP1 also binds to the L domain in EIAV p9, and this binding correlates perfectly with L domain function. These observations identify AIP1 as a component of the viral budding machinery, which serves to link a distinct region in the L domain of HIV-1 p6 and EIAV p9 to ESCRT-III.
cell.com