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

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Vlasak R,Muster T,Lauro AM,Powers JC,Palese P

doi

10.1128/JVI.63.5.2056-2062.1989

subject

Has Abstract

pub_date

1989-05-01 00:00:00

pages

2056-62

issue

5

eissn

0022-538X

issn

1098-5514

journal_volume

63

pub_type

杂志文章