ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2008
A peptide inhibitor of HIV-1 neutralizing antibody 2G12 is not a structural mimic of the natural carbohydrate epitope on gp120.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 33 citations in OpenAlex.
- The development of inovirus-associated vector vaccines using phage-display technologies.Expert review of vaccines · 2019Review
- Review
- Structural basis for enhanced HIV-1 neutralization by a dimeric immunoglobulin G form of the glycan-recognizing antibody 2G12.Cell reports · 2013Article
- Antibody WN1 222-5 mimics Toll-like receptor 4 binding in the recognition of LPS.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Phages and HIV-1: from display to interplay.International journal of molecular sciences · 2012Review
- Potential of peptides as inhibitors and mimotopes: selection of carbohydrate-mimetic peptides from phage display libraries.Journal of nucleic acids · 2012Article
- Engineering filamentous phage carriers to improve focusing of antibody responses against peptides.Vaccine · 2010Article
- Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes.Molecular immunology · 2010Article
- An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies.Journal of virology · 2008Article
- The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design.Microbiology and molecular biology reviews : MMBR · 2008Review
- Developing strategies to enhance and focus humoral immune responses using filamentous phage as a model antigen.Bioengineered bugsArticle
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
MAb 2G12 neutralizes HIV-1 by binding with high affinity to a cluster of high-mannose oligosaccharides on the envelope glycoprotein, gp120. Screening of phage-displayed peptide libraries with 2G12 identified peptides that bind specifically, with K(d)s ranging from 0.4 to 200 microM. The crystal structure of a 21-mer peptide ligand in complex with 2G12 Fab was determined at 2.8 A resolution. Comparison of this structure with previous structures of 2G12-carbohydrate complexes revealed striking differences in the mechanism of 2G12 binding to peptide vs. carbohydrate. The peptide occupies a site different from, but adjacent to, the primary carbohydrate-binding site on 2G12, and makes only slightly fewer contacts to the Fab than Man(9)GlcNAc(2) (51 vs. 56, respectively). However, only two antibody contacts with the peptide are hydrogen bonds in contrast to six with Man(9)GlcNAc(2), and only three of the antibody residues that interact with Man(9)GlcNAc(2) also contact the peptide. Thus, this mechanism of peptide binding to 2G12 does not support structural mimicry of the native carbohydrate epitope on gp120, since it neither replicates the oligosaccharide footprint on the antibody nor most of the contact residues. Moreover, 2G12.1 peptide is not an immunogenic mimic of the 2G12 epitope, since antisera produced against it did not bind gp120.
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Registered trials
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