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  • Title: Binding specificity of influenza C-virus to variably O-acetylated glycoconjugates and its use for histochemical detection of N-acetyl-9-O-acetylneuraminic acid in mammalian tissues.
    Author: Harms G, Reuter G, Corfield AP, Schauer R.
    Journal: Glycoconj J; 1996 Aug; 13(4):621-30. PubMed ID: 8872119.
    Abstract:
    The specificity of influenza C-virus binding to sialoglycoconjugates was tested with various naturally O-acetylated gangliosides or synthetically O-acetylated sialic acid thioketosides, which revealed binding to 9-O-acetylated N-acetylneuraminic acid. Binding was also observed with a sample of Neu5,7Ac2-GD3, however at a lower degree. Sialic acids with two or three O-acetyl groups in the side chain of synthetic sialic acid derivatives are not recognized by the virus. In these experiments, bound viruses were detected with esterase substrates. Influenza C-virus was also used for the histological identification of mono-O-acetylated sialic acids in combination with an immunological visualization of the virus bound to thin-sections. The occurrence of these sialic acids was demonstrated in bovine submandibular gland, rat liver, human normal adult and fetal colon and diseased colon, as well as in human sweat gland. Submandibular gland and colon also contain significant amounts of glycoconjugates with two or three acetyl esters in the sialic acid side chain, demonstrating the value of the virus in discriminating between mono- and higher O-acetylation at the same site. The patterns of staining showed differences between healthy persons and patients with colon carcinoma, ulcerative colitis or Crohn's disease. Remarkably, some human colon samples did not show O-acetyl sialic acid-specific staining. The histochemical observations were controlled by chemical analysis of tissue sialic acids.
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