Multivalent neuraminidase hydrolysis resistant triazole-sialoside protein conjugates as influenza-adsorbents

• DOI: 10.1016/j.cclet.2017.10.032
• Publication Date: 2017-10-27T19:33:44Z
• Authors: Xin Meng; Meibing Yang; Yang Li; Xiaobin Li; Tianwei Jia; Haojie He; Qun Yu; Na Guo; Yun He; Peng Yu; Yang Yang
• Keywords: 0301 basic medicine; 03 medical and health sciences; 3. Good health

Abstract We report the synthesis of pseudo triazole-sialoside protein conjugates of various valency that are resistant to neuraminidase for the adsorption of influenza viruses. The glycotriazole monomer bearing an amine-functionalized linker was synthesized by click chemistry and grafted to the lysine residues of bovine serum albumin (BSA) or human serum albumin (HSA) via diethyl squarate and adipate-based strategy. The binding of hemagglutinin (HA) and neuraminidase (NA) on the virion surface by the synthetic neoglycoproteins were evaluated by hemagglutination and neuraminidase inhibition assay, respectively. The results demonstrated that these synthetic glycoproteins have significantly higher affinity with NA than HA. The interactions between these neoglycoproteins and intact influenza viruses were further investigated by Dynamic Light Scattering (DLS) technique. The pronounced agglutination indicated that these glycoconjugates can be used as adsorbents to prevent virus from invading host cells as well as the release of newly synthesized viral particles, which are crucial in the life cycle of the influenza virus. With the high binding affinity to intact influenza viruses, these neoglycoproteins can also be used as probe to elucidate the molecular mechanism of the sialic acid-influenza recognition and biosensors for influenza detection.