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      hFUT1-Based Live-Cell Assay To Profile α1-2-Fucoside-Enhanced Influenza Virus A Infection.

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          Abstract

          Host cell surface glycans play critical roles in influenza virus A (IVA) infection ranging from modulation of IVA attachment to membrane fusion and host tropism. Approaches for quick and sensitive profile of viral avidity toward a specific type of host cell glycan can contribute to the understanding of tropism switching among different IVA strains. Here, we developed a method based on chemoenzymatic glycan engineering to investigate the possible involvement of α1-2-fucosides in IVA infections. Using a truncated human fucosyltransferase 1 (hFUT1), we created α1-2-fucosides in situ on host cells to assess their influence on the host cell binding to IVA hemagglutinin and the susceptibility of host cells toward IVA-induced killing. We discovered that the newly created α1-2-fucosides on host cells enhanced the infection of several human pandemic IVA subtypes either directly or indirectly. These findings suggest that glycan epitopes other than sialic acid should also be considered for assessing the human pandemic risk of this viral pathogen.

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          Author and article information

          Journal
          ACS Chem Biol
          ACS chemical biology
          American Chemical Society (ACS)
          1554-8937
          1554-8929
          Apr 17 2020
          : 15
          : 4
          Affiliations
          [1 ] Department of Molecular Medicine, The Scripps Research Institute, La Jolla, California 92037, United States.
          [2 ] Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.
          [3 ] School of Medicine, Nankai University, Tianjin 300071, China.
          [4 ] Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, United States.
          [5 ] International Institute of Rare Sugar Research and Education, Kagawa University, Miki, Kagawa 761-0795, Japan.
          Article
          NIHMS1631677
          10.1021/acschembio.9b00869
          7521629
          32271008
          62f3eb5a-c7b6-438f-aedb-fdd653a973a3
          History

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