TY - JOUR
T1 - HIV-1 Assembly
T2 - Viral Glycoproteins Segregate Quantally to Lipid Rafts that Associate Individually with HIV-1 Capsids and Virions
AU - Leung, Kwanyee
AU - Kim, Jae Ouk
AU - Ganesh, Lakshmanan
AU - Kabat, Juraj
AU - Schwartz, Owen
AU - Nabel, Gary J.
PY - 2008/5/15
Y1 - 2008/5/15
N2 - HIV-1 assembly depends on its structural protein, Gag, which after synthesis on ribosomes, traffics to the late endosome/plasma membrane, associates with HIV Env glycoprotein, and forms infectious virions. While Env and Gag migrate to lipid microdomains, their stoichiometry and specificity of interaction are unknown. Pseudotyped viral particles can be made with one viral core surrounded by heterologous envelope proteins. Taking advantage of this property, we analyzed the association of HIV Env and Ebola glycoprotein (GP), with HIV-1 Gag coexpressed in the same cell. Though both viral glycoproteins were expressed, each associated independently with Gag, giving rise to distinct virion populations, each with a single glycoprotein type. Confocal imaging demonstrated that Env and GP localized to distinct lipid raft microdomains within the same cell where they associated with different virions. Thus, a single Gag particle associates "quantally" with one lipid raft, containing homogeneous trimeric viral envelope proteins, to assemble functional virions.
AB - HIV-1 assembly depends on its structural protein, Gag, which after synthesis on ribosomes, traffics to the late endosome/plasma membrane, associates with HIV Env glycoprotein, and forms infectious virions. While Env and Gag migrate to lipid microdomains, their stoichiometry and specificity of interaction are unknown. Pseudotyped viral particles can be made with one viral core surrounded by heterologous envelope proteins. Taking advantage of this property, we analyzed the association of HIV Env and Ebola glycoprotein (GP), with HIV-1 Gag coexpressed in the same cell. Though both viral glycoproteins were expressed, each associated independently with Gag, giving rise to distinct virion populations, each with a single glycoprotein type. Confocal imaging demonstrated that Env and GP localized to distinct lipid raft microdomains within the same cell where they associated with different virions. Thus, a single Gag particle associates "quantally" with one lipid raft, containing homogeneous trimeric viral envelope proteins, to assemble functional virions.
KW - MICROBIO
KW - PROTEINS
UR - http://www.scopus.com/inward/record.url?scp=43049168496&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=43049168496&partnerID=8YFLogxK
U2 - 10.1016/j.chom.2008.04.004
DO - 10.1016/j.chom.2008.04.004
M3 - Article
C2 - 18474355
AN - SCOPUS:43049168496
SN - 1931-3128
VL - 3
SP - 285
EP - 292
JO - Cell Host and Microbe
JF - Cell Host and Microbe
IS - 5
ER -