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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction

Zhiwen He1, Wenyan Zhang, Gongying Chen

  • 1Second Affiliated Hospital, Cancer Institute, School of Medicine, Zhejiang University, Zhejiang, China.

Journal of Molecular Biology
|July 16, 2008
PubMed

Insights

Human immunodeficiency virus (HIV) Vif protein suppresses APOBEC3 antiviral activity by targeting APOBEC3G (A3G) and APOBEC3F (A3F) for degradation. New motifs in Vif are crucial for this interaction and suppression, offering potential targets for novel inhibitors.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Apolipoprotein B mRNA-editing catalytic polypeptide-like 3G (APOBEC3G, or A3G) and APOBEC3F (A3F) are key cellular inhibitors of retroviral replication.
  • Human immunodeficiency virus (HIV) infection requires the viral infectivity factor (Vif) to counteract these APOBEC3 proteins.

Purpose of the Study:

  • To characterize the domains within HIV-1 Vif responsible for recognizing and suppressing APOBEC3 proteins.
  • To identify novel motifs in Vif essential for interaction with and degradation of A3G and A3F.

Main Methods:

  • Mutational analysis of HIV-1 Vif protein domains.
  • Assays to measure Vif-APOBEC3 interaction, protein degradation, and antiviral activity.
  • Sequence conservation analysis of Vif motifs across primate lentiviruses.

Main Results:

  • A novel VxIPLx(4-5)LxPhix(2)YWxL motif (amino acids 52-72) in Vif is essential for A3G interaction, degradation, and antiviral suppression.
  • Interaction with A3G is necessary but not sufficient for Vif's antiviral function.
  • A distinct TGERxW motif (amino acids 74-79) is primarily involved in A3F interaction and inhibition.
  • Both motifs are highly conserved in primate lentiviral Vif proteins.

Conclusions:

  • Primate lentiviral Vif proteins utilize conserved structural motifs to recognize and suppress APOBEC3 proteins.
  • These identified Vif motifs represent potential targets for developing novel antiviral inhibitors against HIV and related viruses.

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