Resistance of Hiv-1 to the Broadly Hiv-1-neutralizing, Anti-carbohydrate Antibody 2g12.
From: Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium.
Virology
- Publish Date: Apr 2007
- ISSN: 0042-6822
- Volume: 360
- Issue: 2
- Pages: 294-304
- Medium: Print
- Language: English
- Citation (JAMA): Huskens Dana, Van Laethem Kristel, Vermeire Kurt, et al. Resistance of Hiv-1 to the Broadly Hiv-1-neutralizing, Anti-carbohydrate Antibody 2g12.. Virology Apr 2007;360:294-304
Abstract
The 2G12 mAb inhibits the infection of HIV-1 laboratory-adapted viruses at 50% inhibitory concentrations (IC(50)) ranging from 0.02 to 0.2 microg/ml when evaluated in different cell-types. However, isolates from various HIV-1 subtypes (such as clade C, D, A/E, F and group O) were not inhibited by 2G12 mAb (IC(50) >20 microg/ml). 2G12 mAb pressure in HIV-1 IIIB- and NL4.3-infected T cell cultures selected for resistant viruses containing only few (1 to 3 N-glycosylation) deletions in gp120. The 2G12-resistant viruses keep their full sensitivity to various mannose-specific lectins and other known HIV entry inhibitors. Moreover, we observed that the NL4.3-2G12-resistant virus, with the N295K mutation in gp120, became significantly more sensitive to several mannose-specific lectins. This is, to our knowledge, the first report showing that a resistant virus generated in vitro against a neutralizing mAb and containing a mutation in gp120, has increased sensitivity to another class of HIV entry inhibitors.
Mesh Headings (Keywords): Amino Acid Substitution, Antibodies, Monoclonal, Cell Line, Cells, Cultured, HIV Antibodies, HIV Envelope Protein gp120, HIV-1, Humans, Models, Molecular, Mutation, Neutralization Tests, Selection (Genetics)
Check for Full Text / PubMed Unique Identifier (PMID): 17123566
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