Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor.

Abstract

In cells infected by HIV-1 mutants lacking a functional Vif protein, APOBEC3G is specifically packaged into progeny virions and then interferes with the process of virus infection. Here, we show that incorporation of APOBEC3G into HIV-1 virions is mediated by the specific interaction of APOBEC3G with the carboxy-terminal nucleocapsid/p6 domain of the Gag polyprotein precursor. As a result, HIV-1 virus-like particles that lack the nucleocapsid domain fail to package APOBEC3G. Surprisingly, RNA was also found to be essential for formation of the nucleocapsid--APOBEC3G complex in vitro, thus raising the possibility that RNA may form a bridge between these two proteins.

• Authors: Alexandra Schäfer, Hal P Bogerd, Bryan R Cullen
• Journal: Virology (Virology) Vol. 328 Issue 2 Pg. 163-8 (Oct 25 2004) ISSN: 0042-6822 [Print] United States
• PMID: 15464836 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Gene Products, gag
• Gene Products, vif
• Protein Precursors
• Proteins
• RNA, Viral
• Repressor Proteins
• vif Gene Products, Human Immunodeficiency Virus
• Nucleoside Deaminases
• APOBEC-3G Deaminase
• APOBEC3G protein, human
• Cytidine Deaminase

Topics

• APOBEC-3G Deaminase
• Cell Line, Transformed
• Cytidine Deaminase
• Gene Products, gag (metabolism)
• Gene Products, vif (genetics)
• HIV-1 (genetics, physiology)
• Nucleocapsid (metabolism)
• Nucleoside Deaminases
• Protein Precursors (metabolism)
• Protein Structure, Tertiary
• Proteins (metabolism)
• RNA, Viral (metabolism)
• Repressor Proteins
• Virion (physiology)
• Virus Assembly
• vif Gene Products, Human Immunodeficiency Virus