Antibody phage display is a powerfulmethod for identification of antibodies with diagnostic, research,and therapeutic applications.  Recently, it has been shown that phagedisplay libraries in which chemical diversity of antibodycomplementarity regions (CDRs) is limited to binomial variation amongtyrosine and serine (Y/S) are sufficient for identification of highaffinity antibodies against a variety of antigens.  Here we have usedY/S libraries to target '5-helix', a mimic of the prehairpinintermediate conformation of HIV-1 gp41.  This is the first knownapplication of Y/S libraries for identification of potential HIV-1fusion inhibitors.  Several nanomolar affinity clones have beenisolated from panning against 5-helix.  We are currentlycharacterizing the neutralization activity of these clones and willanalyze their structures by X-ray crystallography.  Elucidation ofhow Y/S composition and length of CDRs affects these evolvedantibody-antigen interactions will contribute to our understanding ofstructural and functional requirements for viral neutralization.

Targeting HIV-1 gp41 with restricted
diversity phage-displayed antibody libraries

241st National Meeting (2011)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Targeting HIV-1 gp41 with restricted diversity phage-displayed antibody libraries