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-functi...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 （HA） 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.展开更多
基金financially supported by the National Natural Science Foundation of China(Nos.21402140,21502139)Shenzhen Peacock Plan(No. KQTD2016053114253158)+3 种基金Natural Science Foundation of Tianjin City(No. 16JCTPJC46000)Key Laboratory of Industrial Fermentation Microbiology of Ministry of EducationTianjin Key Lab of Industrial Microbiology(No. 2015IM107)Youth Innovation Research Foundation of Tianjin University of Science and Technology(No.2016LG08)
文摘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 （HA） 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.
