Modification of sialic acids by 9-O-acetylation is detected in human leucocytes using the lectin property of influenza C virus |
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Authors: | Zimmer Gert; Suguri Toshiaki; Reuter Gerd; Yu Robert K; Schauer Roland; Herrler Georg |
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Institution: | Institut für Virologie, Philipps-Universitäl, Robert-Koch-Straße 17, D-35037 Marburg
1Biochemisches Institut, Christian-Albrechts-Universität Olshausenstraße 40, D-24098 Kiel, FRG
2Department of Biochemistry, Medical College of Virginia VA 23298-0614, USA |
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Abstract: | Influenza C virus spike glycoprotein HEF specifically recognizesglycoconjugates containing 9-O-acetyl-N-acetylneuraminic acid.The same protein also contains an esterase activity. Takingadvantage of these two properties, influenza C virus was usedas a very sensitive probe for the detection of traces of 9-O-acetyl-N-acetylneuraminicacid in human leucocytes. The binding of influenza C virus toleucocyte glycoproteins and gangliosides separated by sodiumdodecyl sulphatepolyacrylamide gel electrophoresis andthin-layer chromatography, respectively, was assayed using achromogenic esterase substrate. In this way, glycoproteins ofB-lymphocytes and T-lymphocytes were found to contain 9-O-acetylatedsialic acids. Of the various 9-O-acetylated gangliosides detected,one had the characteristics of 9-O-acetylated GD3. The identificationof 9-O-acetylated sialic acids on distinct glycoproteins andglycolipids should be helpful in assigning a physiological roleto this sugar. O-acetylation gangliosides influenza C virus lymphocytes sialic acids |
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