title: Cryoelectron microscopic examination of human immunodeficiency virus type 1 virions with mutations in the cyclophilin A binding loop.
abstract: The human immunodeficiency virus type 1 capsid protein contains a conserved P217X4PX2PX5P231 motif. Mutation at Pro-222 decreases virion incorporation of cyclophilin A, while mutation at Pro-231 abolishes infectivity. Although viral RNA incorporation and protease cleavage of the Gag precursor were not affected by these mutations, cryoelectron microscopy revealed a loss of virion maturation in P231A particles.
authors.affiliation: Department of Molecular and Medical Pharmacology and Crump Institute for Biological Imaging, UCLA School of Medicine, Los Angeles, California 90095, USA.
authors.forename: L B
authors.initials: LB
authors.lastname: Kong
authors.forename: D
authors.initials: D
authors.lastname: An
authors.forename: B
authors.initials: B
authors.lastname: Ackerson
authors.forename: J
authors.initials: J
authors.lastname: Canon
authors.forename: O
authors.initials: O
authors.lastname: Rey
authors.forename: I S
authors.initials: IS
authors.lastname: Chen
authors.forename: P
authors.initials: P
authors.lastname: Krogstad
authors.forename: P L
authors.initials: PL
authors.lastname: Stewart
mesh_terms: D001665:Binding Sites; D002460:Cell Line; D010450:Endopeptidases / Q000378:metabolism; D015683:Gene Products, gag / Q000378:metabolism; D015497:HIV-1 / Q000235:genetics* / Q000378:metabolism / Q000502:physiology / Q000648:ultrastructure*; D006801:Humans; D008854:Microscopy, Electron; D016297:Mutagenesis, Site-Directed; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D014771:Virion / Q000648:ultrastructure; D014779:Virus Replication
chemical_list: D015683:Gene Products, gag; D010450:Endopeptidases; D019696:Peptidylprolyl Isomerase