Toward Fully Synthetic Carbohydrate-Based HIV Antigen Design: On the Critical Role of Bivalency

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• 作者：Vadim Y. Dudkin ; Marianna Orlova ; Xudong Geng ; Mihirbaran Mandal ; William C. Olson ; and Samuel J. Danishefsky
• 刊名：Journal of the American Chemical Society
• 出版年：2004
• 出版时间：August 11, 2004
• 年：2004
• 卷：126
• 期：31
• 页码：9560 - 9562
• 全文大小：158K
• 年卷期：v.126,no.31(August 11, 2004)
• ISSN：1520-5126

文摘

Synthetic gp120^331-335 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.