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. 1994 Aug 2;91(16):7782–7786. doi: 10.1073/pnas.91.16.7782

9-O-acetylated sialic acids have widespread but selective expression: analysis using a chimeric dual-function probe derived from influenza C hemagglutinin-esterase.

A Klein 1, M Krishna 1, N M Varki 1, A Varki 1
PMCID: PMC44486  PMID: 8052660

Abstract

While 9-O-acetylation of sialic acids has been reported in some mammalian tissues, the distribution of this modification on specific cell types and molecules is largely unknown. The influenza C virus hemagglutinin-esterase is a membrane-bound glycoprotein that binds specifically to 9-O-acetylated sialic acids (hemagglutinin activity) and then hydrolyzes the O-acetyl group (receptor-destroying activity). A recombinant soluble form of influenza C virus hemagglutinin-esterase wherein the C-terminal transmembrane and cytoplasmic domains are replaced by the Fc portion of human IgG retains both its recognition and enzymatic functions. The latter activity can selectively remove 9-O-acetyl groups from bound or free sialic acids and, under specific conditions, 7-O-acetyl groups as well. Irreversible inactivation of the esterase unmasks stable recognition activity, giving a molecule that binds specifically to 9-O-acetylated sialic acids. These probes demonstrate widespread but selective expression of 9-O-acetylated sialic acids in certain cell types of rat tissues. Patterns of polarized or gradient expression further demonstrate the regulated nature of this modification. Direct probing of blots and thin-layer plates shows selective expression of 9-O-acetylation on certain glycoproteins and glycolipids in such tissues. Thus, 9-O-acetylation is more widespread than previously thought and occurs on specific molecules and cell types.

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