title: Sialic acid and sialyl-lactose glyco-conjugates: design, synthesis and binding assays to lectins and swine influenza H1N1 virus.
abstract: The terminal parts of the influenza hemagglutinin (HA) receptors α2,6- and α2,3-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 α2,6-sialyllactose is specifically recognized by the biotinylated Sambucus nigra (elderberry) bark lectin, which binds preferentially to sialic acid in an α2,6-linkage. SOC(4) -glyco-conjugate bearing two copies of the α2,3-sialyllactose was not recognized by the biotinylated Maackia amurensis lectin, despite its well-known α2,3-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.
authors: Department of Chemistry, Section of Organic Chemistry and Biochemistry, University of Ioannina, 45110, Ioannina, Greece. stella.zevgiti@gmail.com
authors: Stella
authors: S
authors: Zevgiti
authors: Juliana Gonzalez
authors: JG
authors: Zabala
authors: Ayub
authors: A
authors: Darji
authors: Ursula
authors: U
authors: Dietrich
authors: Eugenia
authors: E
authors: Panou-Pomonis
authors: Maria
authors: M
authors: Sakarellos-Daitsiotis
mesh_terms: D001681:Biological Assay; D003101:Collodion / Q000737:chemistry; D006001:Glycoconjugates / Q000138:chemical synthesis* / Q000378:metabolism; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D053118:Influenza A Virus, H1N1 Subtype / Q000737:chemistry* / Q000378:metabolism; D007251:Influenza, Human / Q000821:virology; D007785:Lactose / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D018716:Molecular Mimicry; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D037121:Plant Lectins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*; D027924:Sambucus nigra / Q000737:chemistry; D012794:Sialic Acids / Q000138:chemical synthesis* / Q000378:metabolism; D060327:Solid-Phase Synthesis Techniques; D053586:Virus Internalization
chemical_list: C403777:6'-sialyllactose; D006001:Glycoconjugates; C543345:H1N1 virus hemagglutinin; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D009842:Oligopeptides; D037121:Plant Lectins; D011991:Receptors, Virus; D012794:Sialic Acids; D003101:Collodion; D007785:Lactose