Cryoelectron microscopic examination of human immunodeficiency virus type 1 virions with mutations in the cyclophilin A binding loop.
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.
Kong
L B
LB
Department of Molecular and Medical Pharmacology and Crump Institute for Biological Imaging, UCLA School of Medicine, Los Angeles, California 90095, USA.
An
D
D
Ackerson
B
B
Canon
J
J
Rey
O
O
Chen
I S
IS
Krogstad
P
P
Stewart
P L
PL
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
D015683:Gene Products, gag; D010450:Endopeptidases; D019696:Peptidylprolyl Isomerase