Affinity maturation and characterization of a human monoclonal antibody against HIV-1 gp41

The human D5 monoclonal antibody binds to the highly conserved hydrophobic pocket on the N-terminal heptad repeat (NHR) trimer of HIV-1 gp41 and exhibits modest yet relatively broad neutralization activity. Both binding and neutralization depend on residues in the complementarity determining regions...

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Veröffentlicht in:	mAbs 2009-09, Vol.1 (5), p.462-474
Hauptverfasser:	Montgomery, Donna L., Wang, Ying-Jie, Hrin, Renee, Luftig, Micah, Su, Bin, Miller, Michael D., Wang, Fubao, Haytko, Peter, Huang, Lingyi, Vitelli, Salvatore, Condra, Jon, Liu, Xiaomei, Hampton, Richard, Carfi, Andrea, Pessi, Antonello, Bianchi, Elisabetta, Joyce, Joseph, Lloyd, Chris, Geleziunas, Romas, Bramhill, David, King, Vicki M., Finnefrock, Adam C., Strohl, William, An, Zhiqiang
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - immunology Antibodies, Neutralizing - chemistry Antibodies, Neutralizing - immunology Antibody Affinity - immunology Binding Biology Bioscience Calcium Cancer Cell Complementarity Determining Regions - chemistry Cycle HIV Antibodies - chemistry HIV Antibodies - immunology HIV Envelope Protein gp41 - immunology HIV-1 - immunology Humans Immunoglobulin Fragments - immunology Immunoglobulin G - chemistry Immunoglobulin G - immunology Landes Molecular Sequence Data Neutralization Tests Organogenesis Peptide Library Proteins
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