title: Cell-free systems for capsid assembly of primate lentiviruses from three different lineages.
abstract: We recently demonstrated that capsids from three main primate lentiviral lineages appear to form via a pathway of assembly intermediates in primate cells. Retroviral capsid assembly intermediates were initially identified and characterized using a cell-free system for assembly of immature HIV-1 capsids. Because cell-free capsid assembly systems are useful tools, we are interested in developing such systems for other primate lentiviruses besides HIV-1. Here we extend previous cell-free studies by showing that Gag proteins of HIV-2, from a second primate lentiviral lineage, progress from early intermediates to late intermediates and completed capsids over time. Additionally, we demonstrate that Gag proteins of SIVagm, from a third primate lentiviral lineage, associate with the cellular factor HP68 and complete assembly in this system. Therefore, cell-free systems reproduce assembly of Gag from three main primate lentiviral lineages, and can be used to compare mechanistic features of capsid assembly of genetically divergent primate lentiviruses.
authors.affiliation: Department of Pathobiology, University of Washington, Seattle, WA, USA. jais@u.washington.edu
authors.forename: Julia E
authors.initials: JE
authors.lastname: Dooher
authors.forename: Jaisri R
authors.initials: JR
authors.lastname: Lingappa
mesh_terms: D000818:Animals; D019556:COS Cells; D036022:Capsid Proteins / Q000378:metabolism*; D002474:Cell-Free System; D002499:Centrifugation, Density Gradient; D002522:Chlorocebus aethiops; D015683:Gene Products, gag / Q000378:metabolism*; D015498:HIV-2 / Q000378:metabolism / Q000502:physiology*; D047468:Immunoprecipitation; D010957:Plasmids; D014158:Transcription, Genetic; D019065:Virus Assembly
chemical_list: D036022:Capsid Proteins; D015683:Gene Products, gag