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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/25513

Title: Investigation of a Putative Secondary Binding Site between the Broadly Neutralizing Monoclonal anti-HIV-1 Antibody and its Antigen gp41
Authors: Wierzbicka, Marta
Advisor: Pai, Emil F.
Department: Biochemistry
Keywords: HIV-1
broadly neutralizing antibodies
gp41
2F5 Fab
Issue Date: 30-Dec-2010
Abstract: One potential approach to vaccine development against HIV involves generating an immunogen that can elicit the production of broadly neutralizing monoclonal antibodies (bnmAbs), which target specific sites on the HIV-1 envelope. Using site-directed mutagenesis and ELISA assays, this thesis investigates the idea of a secondary binding site of one of the bnmAbs, 2F5, as suggested by previous studies that identified residues Asp64, Thr65, and Arg82B on 2F5 that are recognized by its anti-idiotypic antibody 3H6. Results show that 2F5 binds only very weakly to the gp41 ectodomain in its post-fusion conformation. However, a small but significant difference was observed between the binding of the mutants and the T-20 peptide, a fusion inhibiting drug. Due to the limited effect, the results need to be confirmed using more quantitative techniques and more optimal conformations of the antigen, but raise the prospect that design of immunogens to elicit HIV-specific antibodies might have to incorporate this novel interaction site.
URI: http://hdl.handle.net/1807/25513
Appears in Collections:Master
Department of Biochemistry - Master theses

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