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Science 5 June 1987: Vol. 236. no. 4806, pp. 1293 - 1295 DOI: 10.1126/science.3589663
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Articles
Science, Vol 236, Issue 4806, 1293-1295
Copyright © 1987 by American Association for the Advancement of Science
Selective inactivation of influenza C esterase: a probe for detecting 9-O-acetylated sialic acids
EA Muchmore
and
A Varki
The influenza C virus (INF-C) hemagglutinin recognizes 9-O-acetyl-N-acetylneuraminic acid. The same protein contains the receptor-destroying enzyme (RDE), which is a 9-O-acetyl-esterase. The RDE was inactivated by the serine esterase inhibitor di-isopropyl fluorophosphate (DFP). [3H]DFP-labeling localized the active site to the heavy chain of the glycoprotein. DFP did not alter the hemagglutination or fusion properties of the protein, but markedly decreased infectivity of the virus, demonstrating that the RDE is important for primary infection. Finally, DFP-treated INF-C bound specifically and irreversibly to cells expressing 9-O-acetylated sialic acids. This provides a probe for a molecule that was hitherto very difficult to study.
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