Sialic acid and sialyl-lactose glyco-conjugates: design, synthesis and binding assays to lectins and swine influenza H1N1 virus

✍ Scribed by Stella Zevgiti; Juliana Gonzalez Zabala; Ayub Darji; Ursula Dietrich; Eugenia Panou-Pomonis; Maria Sakarellos-Daitsiotis

• Publisher: John Wiley and Sons
• Year: 2011
• Tongue: English
• Weight: 242 KB
• Volume: 18
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.1415

✦ Synopsis

The terminal parts of the influenza hemagglutinin (HA) receptors __α__2,6‐ and α__2,3‐sialyllactoses were conjugated to an artificial carrier, named sequential oligopeptide carrier (SOC~4~), to formulate human and avian receptor mimics, respectively. SOC~4~, formed by the tripeptide unit Lys‐Aib‐Gly, adopts a rigid helicoids‐type conformation, which enables the conjugation of biomolecules to the Lys‐N^ε^__H~2~ groups. By doing so, it preserves their initial conformations and functionalities of the epitopes. We report that SOC~4~‐glyco‐conjugate bearing two copies of the __α__2,6‐sialyllactose is specifically recognized by the biotinylated Sambucus nigra (elderberry) bark lectin, which binds preferentially to sialic acid in an __α__2,6‐linkage. SOC~4~‐glyco‐conjugate bearing two copies of the __α__2,3‐sialyllactose was not recognized by the biotinylated Maackia amurensis lectin, despite its well‐known __α__2,3‐sialyl bond specificity. However, preliminary immune blot assays showed that H1N1 virus binds to both the SOC~4~‐glyco‐conjugates immobilized onto nitrocellulose membrane. It is concluded that Ac‐SOC~4~[(Ac)~2~,(3′SL‐Aoa)~2~]‐NH~2~ 5 and Ac‐SOC~4~[(Ac)~2~,(6′SL‐Aoa)~2~]‐NH~2~ 6 mimic the HA receptors. These findings could be useful for easy screening of binding and inhibition assays of virus–receptor interactions. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.