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

Journal Article · Mon May 01 00:00:00 EDT 1989 · J. Virol.; (United States)

OSTI ID:6076308

Vlasak, R; Muster, T; Lauro, A M; Powers, J C; Palese, P

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 /sup 3/H-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, the authors suggest that this viral enzyme is a serine hydrolase constituting a new family of serine esterases. Furthermore, they 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.

• Research Organization: Mount Sinai School of Medicine, New York, NY (USA)
• OSTI ID: 6076308
• Journal Information: J. Virol.; (United States), Vol. 63:5
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ESTERASES
AMINO ACID SEQUENCE
INFLUENZA VIRUSES
INFECTIVITY
VIRAL DISEASES
PATHOGENESIS
BIOLOGICAL FUNCTIONS
ENZYME INHIBITORS
ERYTHROCYTES
INHIBITION
MOLECULAR BIOLOGY
TRACER TECHNIQUES
TRITIUM COMPOUNDS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
DISEASES
ENZYMES
FUNCTIONS
HYDROLASES
INFECTIOUS DISEASES
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MATERIALS
MICROORGANISMS
MOLECULAR STRUCTURE
PARASITES
VIRUSES
550201* - Biochemistry- Tracer Techniques
550901 - Pathology- Tracer Techniques