| Literature DB >> 15168796 |
Mei-Yun Zhang1, Yuuei Shu, Igor Sidorov, Dimiter S Dimitrov.
Abstract
A new human monoclonal antibody (hmAb), designated m16, was selected by sequential antigen panning (SAP) of a human phage display library against recombinant soluble HIV-1 envelope glycoproteins (Envs) (gp140s) and their complexes with soluble CD4. It bound with high (nM) affinity to gp120 and gp140; the binding was further enhanced by interactions of the Envs with CD4. m16 inhibited cell fusion mediated by the Envs of 9 HIV-1 isolates from clades A, B, E and G with potency on average comparable to that of the broadly neutralizing human monoclonal antibody Fab X5. The identification of a new hmAb with broad neutralizing activity that exhibits differential inhibitory profile suggests a potential for its use as a component of anti-HIV-1 treatments.Entities:
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Year: 2004 PMID: 15168796 DOI: 10.1016/j.antiviral.2003.09.009
Source DB: PubMed Journal: Antiviral Res ISSN: 0166-3542 Impact factor: 5.970