title: [Membrane Binding of Retroviral Gag Proteins].
abstract: Location of virus assembly in infected cells has major influences on efficiencies of virus assembly and release and on post-assembly processes including cell-to-cell transmission. Therefore, for better understanding of virus spread and for developing new antiviral strategies, it is important to elucidate mechanisms by which the subcellular site of virus particle assembly is determined. Retrovirus particle assembly is driven by viral structural protein Gag. In the case of HIV-1, Gag binds to the plasma membrane (PM) via the N-terminal MA domain and forms nascent particles at this location. Recent studies reveled that PM-specific phospholipid PI(4,5)P2 plays an important role in directing Gag to the PM through its interaction with MA. In this review, I will summarize our current understanding of relationships between retroviral MA domains and phospholipids in cellular membranes and discuss possible mechanisms by which lipids and other factors regulate membrane binding and subcellular localization of retroviral Gag proteins.
authors.affiliation: Department of Microbiology and Immunology, University of Michigan Medical School.
authors.forename: Akira
authors.initials: A
authors.lastname: Ono
mesh_terms: D000998:Antiviral Agents; D002462:Cell Membrane / Q000378:metabolism* / Q000821:virology*; D055808:Drug Discovery; D015683:Gene Products, gag / Q000737:chemistry / Q000378:metabolism*; D015497:HIV-1 / Q000235:genetics / Q000502:physiology; D010716:Phosphatidylinositols / Q000502:physiology; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012190:Retroviridae / Q000235:genetics* / Q000502:physiology*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*; D019065:Virus Assembly / Q000235:genetics
chemical_list: D000998:Antiviral Agents; D015683:Gene Products, gag; D010716:Phosphatidylinositols; D014764:Viral Proteins