Authors: | Dudkin, V. Y.; Orlova, M.; Geng, X.; Mandal, M.; Olson, W. C.; Danishefsky, S. J. |
Article Title: | Toward fully synthetic carbohydrate-based HIV antigen design: On the critical role of bivalency |
Abstract: | Synthetic gp120331-335 glycopeptide fragments carrying hybrid and high-mannose type N-linked glycans were evaluated for binding to broadly neutralizing antibody 2G12 using surface plasmon resonance technology. None of the hybrid-type constructs demonstrated binding to 2G12. In the high-mannose series, the "Cys dimer" construct, presenting two undecasaccharide glycans, showed significantly higher binding than the Cys-protected monomer. The binding of the dimeric structure was further investigated in competition with recombinant gp120. The data suggest that gp120 and its designed synthetic epitope construct bind to the same site on 2G12. Copyright © 2004 American Chemical Society. |
Keywords: | unclassified drug; human immunodeficiency virus infection; mass spectrometry; drug synthesis; immune response; molecular sequence data; peptide fragments; vaccine production; liquid chromatography; surface plasmon resonance; carbohydrate sequence; carbohydrates; glycopeptide; glycopeptides; disulfide; carbohydrate; chitobiose; oligosaccharide; glycan; human immunodeficiency virus vaccine; hiv envelope protein gp120; virus envelope protein; mannose; glycoprotein gp 120; article; glycosidase; human immunodeficiency virus antibody; human immunodeficiency virus antigen; hiv antigens |
Journal Title: | Journal of the American Chemical Society |
Volume: | 126 |
Issue: | 31 |
ISSN: | 0002-7863 |
Publisher: | American Chemical Society |
Date Published: | 2004-08-11 |
Start Page: | 9560 |
End Page: | 9562 |
Language: | English |
DOI: | 10.1021/ja047720g |
PROVIDER: | scopus |
PUBMED: | 15291558 |
DOI/URL: | |
Notes: | J. Am. Chem. Soc. -- Cited By (since 1996):67 -- Export Date: 16 June 2014 -- CODEN: JACSA -- Source: Scopus |