PMID: 2495370May 1, 1989Paper

Influenza C virus esterase: analysis of catalytic site, inhibition, and possible function

Journal of Virology
Reinhard VlasakP Palese

Abstract

The active site serine of the acetylesterase of influenza C virus was localized to amino acid 71 of the hemagglutinin-esterase protein by affinity labeling with 3H-labeled diisopropylfluorophosphate. This serine and the adjacent amino acids (Phe-Gly-Asp-Ser) are part of a consensus sequence motif found in serine hydrolases. Since comparative analysis failed to reveal esterase sequence similarities with other serine hydrolases, we suggest that this viral enzyme is a serine hydrolase constituting a new family of serine esterases. Furthermore, we found that the influenza C virus esterase was inhibited by isocoumarin derivatives, with 3,4-dichloroisocoumarin being the most potent inhibitor. Addition of this compound prevented elution of influenza C virus from erythrocytes and inhibited virus infectivity, possibly through inhibition of virus entry into cells.

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Citations

Jun 7, 1996·The Journal of Biological Chemistry·M J GuimarãesA Zlotnik
Apr 16, 2005·The Journal of General Virology·Andrea HanikaGert Zimmer
Oct 16, 2010·Glycobiology·Sigrid ArmingReinhard Vlasak
Oct 1, 1995·Virus Research·Y MatsuzakiK Nakamura
Jul 1, 1997·Journal of Virology·L A CornelissenR J de Groot
Jun 23, 2021·The Journal of Biological Chemistry·Eline A VisserChristian Büll
Dec 12, 2002·Chemical Reviews·James C PowersKaren Ellis James
Apr 29, 2011·European Journal of Medicinal Chemistry·Mathew StanleyHansjörg Streicher

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