Sialic acid and sialyl-lactose glyco- conjugates: design, synthesis andbinding assays to lectins and swine influenza H1N1 virus
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Zevgiti, S.,
(EN)
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
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Zevgiti, S.,
(EN)
The terminal parts of the influenza hemagglutinin (HA) receptors Ξ±2,6- and Ξ±2,3-sialyllactoses were conjugated to an artificial carrier, named sequential oligopeptide carrier (SOC4), to formulate human and avian receptor mimics, respectively. SOC4, formed by the tripeptide unit Lys-Aib-Gly, adopts a rigid helicoids-type conformation, which enables the conjugation of biomolecules to the Lys-NΞµH2 groups. By doing so, it preserves their initial conformations and functionalities of the epitopes. We report that SOC4-glyco-conjugate bearing two copies of the Ξ±2,6-sialyllactose is specifically recognized by the biotinylated Sambucus nigra (elderberry) bark lectin, which binds preferentially to sialic acid in an Ξ±2,6-linkage. SOC4-glyco-conjugate bearing two copies of the Ξ±2,3-sialyllactose was not recognized by the biotinylated Maackia amurensis lectin, despite its well-known Ξ±2,3-sialyl bond specificity. However, preliminary immune blot assays showed that H1N1 virus binds to both the SOC4-glyco-conjugates immobilized onto nitrocellulose membrane. It is concluded that Ac-SOC4[(Ac)2,(3'SL-Aoa)2]-NH2 5 and Ac-SOC4[(Ac)2,(6'SL-Aoa)2]-NH2 6 mimic the HA receptors. These findings could be useful for easy screening of binding and inhibition assays of virus-receptor interactions.
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