Modification of sialic acids by 9-O-acetylation is detected in human leucocytes using the lectin property of influenza C virus

Gert Zimmer, Toshiaki Suguri, Gerd Reuter, Robert K. Yu, Roland Schauer, Georg Herrler

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Influenza C virus spike glycoprotein HEF specifically recognizes glycoconjugates containing 9-O-acetyl-N-acetylneuraminic acid. The same protein also contains an esterase activity. Taking advantage of these two properties, influenza C virus was used as a very sensitive probe for the detection of traces of 9-O-acetyl-N-acetylneuraminic acid in human leucocytes. The binding of influenza C virus to leucocyte glycoproteins and gangliosides separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and thin-layer chromatography, respectively, was assayed using a chromogenic esterase substrate. In this way, glycoproteins of B-lymphocytes and T-lymphocytes were found to contain 9-O-acetylated sialic acids. Of the various 9-O-acetylated gangliosides detected, one had the characteristics of 9-O-acetylated GD3. The identification of 9-O-acetylated sialic acids on distinct glycoproteins and glycolipids should be helpful in assigning a physiological role to this sugar.

Original languageEnglish (US)
Pages (from-to)343-349
Number of pages7
JournalGlycobiology
Volume4
Issue number3
DOIs
StatePublished - Jun 1 1994
Externally publishedYes

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Keywords

  • Gangliosides
  • Influenza C virus
  • Lymphocytes
  • O-acetylation
  • Sialic acids

ASJC Scopus subject areas

  • Biochemistry

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