title: Preparation of recombinant HIV-1 gag protein and assembly of virus-like particles in vitro.
abstract: The mechanism of assembly of retroviruses is not fully understood. Purification of retroviral Gag protein and studying its solution state and assembly properties might provide insights into retroviral assembly mechanisms. Here we describe a rapid method for the purification of Gag and its subsequent assembly into virus-like particles in a defined system in vitro. The purification scheme does not use affinity tags, but purifies the native protein by virtue of its high affinity for phosphocellulose, a property presumably related to the affinity of Gag proteins for nucleic acids.
authors.affiliation: HIV Drug Resistance Program, National Cancer Institute, Frederick MD, USA.
authors.forename: Siddhartha A K
authors.initials: SA
authors.lastname: Datta
authors.forename: Alan
authors.initials: A
authors.lastname: Rein
mesh_terms: D002474:Cell-Free System; D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D022701:Virosomes / Q000378:metabolism; D019065:Virus Assembly; D054301:gag Gene Products, Human Immunodeficiency Virus / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D022701:Virosomes; D054301:gag Gene Products, Human Immunodeficiency Virus