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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
10:50

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

Published on: September 16, 2010

Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120

D P Weliky1, A E Bennett, A Zvi

  • 1Department of Chemistry, Michigan State University, East Lansing 48824, USA.

Nature Structural Biology
|February 27, 1999
PubMed

Insights

Solid-state NMR reveals the Gly-Pro-Gly-Arg motif of HIV-1 V3 loop peptides adopts antibody-dependent structures. This structural insight into peptide-protein complexes offers new avenues for therapeutic development.

Area of Science:

  • Structural biology
  • Biophysics
  • Immunology

Background:

  • The V3 loop of HIV-1 gp120 is a critical target for neutralizing antibodies.
  • Understanding the conformational dynamics of the V3 loop is essential for vaccine design.

Purpose of the Study:

  • To determine the conformation of the V3 loop's GPGR motif when bound to an anti-gp120 antibody.
  • To investigate the conformational heterogeneity of the V3 loop in unbound gp120.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy on frozen solutions of a peptide-antibody complex.
  • Integration of NMR data with existing crystal structures and antibody cross-reactivity data.

Main Results:

  • Solid-state NMR provided strong constraints on the V3 loop's GPGR motif conformation in the antibody-bound state.
  • The GPGR motif exhibits an antibody-dependent conformation.
  • Evidence suggests conformational heterogeneity of the GPGR motif in unbound gp120.

Conclusions:

  • The study demonstrates the first application of solid-state NMR for structural analysis of peptide-protein complexes.
  • The GPGR motif's conformation is influenced by antibody binding.
  • Conformational flexibility of the V3 loop may be a factor in HIV-1 immune evasion.

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