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Journal of Virology, May 1999, p. 3737-3743, Vol. 73, No. 5
Institute of Molecular Biology, Austrian
Academy of Sciences, A-5020 Salzburg, Austria,1
and University of Leiden, Institute of Microbiology, Department
of Virology, 2300 AH Leiden, The Netherlands2
Received 30 April 1998/Accepted 26 January 1999
We have characterized the hemagglutinin-esterase (HE) of puffinosis
virus (PV), a coronavirus closely related to mouse hepatitis virus
(MHV). Analysis of the cloned gene revealed approximately 85% sequence
identity to HE proteins of MHV and approximately 60% identity to the
corresponding esterase of bovine coronavirus. The HE protein exhibited
acetylesterase activity with synthetic substrates
p-nitrophenyl acetate,
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Identification of a Coronavirus
Hemagglutinin-Esterase with a Substrate Specificity Different from
Those of Influenza C Virus and Bovine Coronavirus
-naphthyl acetate, and
4-methylumbelliferyl acetate. In contrast to other viral esterases, no
activity was detectable with natural substrates containing
9-O-acetylated sialic acids. Furthermore, PV esterase was
unable to remove influenza C virus receptors from human erythrocytes,
indicating a substrate specificity different from HEs of influenza C
virus and bovine coronavirus. Solid-phase binding assays revealed that
purified PV was unable to bind to sialic acid-containing
glycoconjugates like bovine submaxillary mucin, mouse
1
macroglobulin or bovine brain extract. Because of the close
relationship to MHV, possible implications on the substrate specificity
of MHV esterases are suggested.
*
Corresponding author. Mailing address: Institute of
Molecular Biology, Austrian Academy of Sciences, Billroth Str. 11, A-5020 Salzburg, Austria. Phone: 43-662-6396124. Fax:
43-662-6396129. E-mail: rvlasak{at}oeaw.ac.at.
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