Toward fully synthetic carbohydrate-based HIV antigen design: on the critical role of bivalency.
J Am Chem Soc
; 126(31): 9560-2, 2004 Aug 11.
Article
in En
| MEDLINE
| ID: mdl-15291558
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carbohydrates
/
Glycopeptides
/
HIV Antigens
/
HIV Envelope Protein gp120
Language:
En
Journal:
J Am Chem Soc
Year:
2004
Type:
Article
Affiliation country:
United States