HIV-1 Assembly: Viral Glycoproteins Segregate Quantally to Lipid Rafts that Associate Individually with HIV-1 Capsids and Virions

Kwanyee Leung, Jae Ouk Kim, Lakshmanan Ganesh, Juraj Kabat, Owen Schwartz, Gary J. Nabel

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)285-292
Number of pages8
JournalCell Host and Microbe
Volume3
Issue number5
DOIs
StatePublished - May 15 2008
Externally publishedYes

Keywords

  • MICROBIO
  • PROTEINS

ASJC Scopus subject areas

  • Immunology and Microbiology(all)
  • Cancer Research
  • Molecular Biology

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