- Poster presentation
- Open Access
Recombinant Env proteins that bind the quaternary-specific, V1/V2-directed PGT antibodies
© Gorman et al; licensee BioMed Central Ltd. 2012
- Published: 13 September 2012
- Infectious Disease
- Cancer Research
- Recombinant Protein
- Structural Information
- Antibody Binding
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.
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.
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.
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.
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.