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Journal of Virology, June 1999, p. 4721-4727, Vol. 73, No. 6
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Hemagglutinin-Esterase of Mouse Hepatitis Virus Strain S Is a Sialate-4-O-Acetylesterase

Gerhard Regl,1 Alexandra Kaser,1 Matthias Iwersen,2 Hiltrud Schmid,2 Guido Kohla,2 Birgit Strobl,1 Ulrike Vilas,1 Roland Schauer,2 and Reinhard Vlasak1,*

Austrian Academy of Sciences, Institute of Molecular Biology, A-5020 Salzburg, Austria,1 and University of Kiel, Institute of Biochemistry, D-24098 Kiel, Germany2

Received 9 December 1998/Accepted 5 March 1999

By comparative analysis of the hemagglutinin-esterase (HE) protein of mouse hepatitis virus strain S (MHV-S) and the HE protein of influenza C virus, we found major differences in substrate specificities. In striking contrast to the influenza C virus enzyme, the MHV-S esterase was unable to release acetate from bovine submandibulary gland mucin. Furthermore, MHV-S could not remove influenza C virus receptors from erythrocytes. Analysis with free sialic acid derivatives revealed that the MHV-S HE protein specifically de-O-acetylates 5-N-acetyl-4-O-acetyl sialic acid (Neu4,5Ac2) but not 5-N-acetyl-9-O-acetyl sialic acid (Neu5,9Ac2), which is the major substrate for esterases of influenza C virus and bovine coronaviruses. In addition, the MHV-S esterase converted glycosidically bound Neu4,5Ac2 of guinea pig serum glycoproteins to Neu5Ac. By expression of the MHV esterase with recombinant vaccinia virus and incubation with guinea pig serum, we demonstrated that the viral HE possesses sialate-4-O-acetylesterase activity. In addition to observed enzymatic activity, MHV-S exhibited affinity to guinea pig and horse serum glycoproteins. Binding required sialate-4-O-acetyl groups and was abolished by chemical de-O-acetylation. Since Neu4,5Ac2 has not been identified in mice, the nature of potential substrates and/or secondary receptors for MHV-S in the natural host remains to be determined. The esterase of MHV-S is the first example of a viral enzyme with high specificity and affinity toward 4-O-acetylated sialic acids.

* Corresponding author. Mailing address: Austrian Academy of Sciences, Institute of Molecular Biology, Billrothstr. 11, A-5020 Salzburg, Austria. Phone: 43-662-6396124. Fax: 43-662-6396129. E-mail: rvlasak{at}oeaw.ac.at.

Journal of Virology, June 1999, p. 4721-4727, Vol. 73, No. 6
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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