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Volume 9 Supplement 2

AIDS Vaccine 2012

  • Poster presentation
  • Open Access

Recombinant Env proteins that bind the quaternary-specific, V1/V2-directed PGT antibodies

  • 1,
  • 1,
  • 1,
  • 1,
  • 1,
  • 2,
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  • 1
Retrovirology20129 (Suppl 2) :P84

https://doi.org/10.1186/1742-4690-9-S2-P84

  • Published:

Keywords

  • Infectious Disease
  • Cancer Research
  • Recombinant Protein
  • Structural Information
  • Antibody Binding

Background

Antibodies PGT141-145 are broadly neutralizing and recognize a glycan-dependent epitope in the V1/V2 loop, similar to antibodies PG9 and PG16. Collectively, this class of antibodies binds preferentially to the functional viral spike. Although PG9, and to a lesser extent, PG16, bind monomeric gp120s and V1/V2 scaffolds, to date no recombinant env-derived proteins have been identified that bind to antibodies PGT141-145.

Methods

As a first step toward obtaining structural information of the epitope recognized by PGT141-145, we have created and characterized novel gp140s and epitope scaffolds designed to present the V1/V2 conformation recognized by PGT141-145. To date, over 70 recombinant proteins have been expressed and tested for antibody binding.

Results

We have identified one V1/V2-scaffold protein that binds to PGT142. The binding is dependent on the HIV-1 strain used in the scaffold. We have also produced trimeric, cleaved gp140 constructs and evaluated them for binding to PGT141-145.

Conclusion

Proteins that accurately mimic V1/V2 conformations of the functional viral spike are crucial to obtaining structures of the PGT antibodies in complex with their epitopes, and may be ideal immunogens for eliciting broadly neutralizing, V1/V2-directed antibodies in a vaccine setting.

Authors’ Affiliations

(1)
National Institutes of Health, Bethesda, MD, USA
(2)
Avatar Biotechnologies, Brooklyn, NY, USA

Copyright

© Gorman et al; licensee BioMed Central Ltd. 2012

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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