APOBEC3G incorporation into human immunodeficiency virus type 1 particles.
APOBEC3G is promiscuous with respect to its antiretroviral effect, requiring that it be packaged into diverse retrovirus particles. Here, we show that most virally encoded human immunodeficiency virus type 1 particle components are dispensable for APOPEC3G incorporation. However, replacement of the nucleocapsid (NC) Gag domain with a leucine zipper abolished APOBEC3G incorporation. Moreover, coprecipitation analysis showed that APOBEC3G-Gag interaction requires NC and nonspecific RNA. These observations suggest that APOBEC3G exploits an essential property of retroviruses, namely, RNA packaging, to infiltrate particles. Because it is, therefore, difficult to evolve specific sequences that confer escape from APOBEC3G, these findings may explain why lentiviruses evolved an activity that induces its destruction.
Aaron Diamond AIDS Research Center and the Rockefeller University, New York, NY 10016, USA.
Véronique
V
Zennou
David
D
Perez-Caballero
Heinrich
H
Göttlinger
Paul D
PD
Bieniasz
D000071480:APOBEC-3G Deaminase; D003564:Cytidine Deaminase; D015683:Gene Products, gag / Q000502:physiology; D015497:HIV-1 / Q000378:metabolism*; D009700:Nucleoside Deaminases; D011506:Proteins / Q000378:metabolism*; D012367:RNA, Viral / Q000502:physiology; D012097:Repressor Proteins; D014771:Virion / Q000378:metabolism*; D019065:Virus Assembly
D015683:Gene Products, gag; D011506:Proteins; D012367:RNA, Viral; D012097:Repressor Proteins; D009700:Nucleoside Deaminases; D000071480:APOBEC-3G Deaminase; C464924:APOBEC3G protein, human; D003564:Cytidine Deaminase