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J. Biol. Chem., Vol. 280, Issue 8, 6933-6941, February 25, 2005

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Nidovirus Sialate-O-Acetylesterases

EVOLUTION AND SUBSTRATE SPECIFICITY OF CORONAVIRAL AND TOROVIRAL RECEPTOR-DESTROYING ENZYMES^*

Saskia L. Smits, Gerrit J. Gerwig, Arno L. W. van Vliet, Arjen Lissenberg¶, Peter Briza||, Johannis P. Kamerling**, Reinhard Vlasak¶¶, and Raoul J. de Groot||||

From the Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, 3584 CL Utrecht, and Bijvoet Center for Biomolecular Research, Department of Bio-Organic Chemistry, Section of Glycoscience and Biocatalysis, Utrecht University, 3584 CH Utrecht, The Netherlands, the ^||Department of Molecular Biology and Applied Biotechnology, Department of Cell Biology, University of Salzburg, A-5020 Salzburg, Austria

Many viruses achieve reversible attachment to sialic acid (Sia) by encoding envelope glycoproteins with receptor-binding and receptor-destroying activities. Toroviruses and group 2 coronaviruses bind to O-acetylated Sias, presumably via their spike proteins (S), whereas other glycoproteins, the hemagglutinin-esterases (HE), destroy Sia receptors by de-O-acetylation. Here, we present a comprehensive study of these enzymes. Sialate-9-O-acetylesterases specific for 5-N-acetyl-9-O-acetylneuraminic acid, described for bovine and human coronaviruses, also occur in equine coronaviruses and in porcine toroviruses. Bovine toroviruses, however, express novel sialate-9-O-acetylesterases, which prefer the di-O-acetylated substrate 5-N-acetyl-7(8),9-di-O-acetylneuraminic acid. Whereas most rodent coronaviruses express sialate-4-O-acetylesterases, the HE of murine coronavirus DVIM cleaves 9-O-acetylated Sias. Under the premise that HE specificity reflects receptor usage, we propose that two types of Sias serve as initial attachment factors for coronaviruses in mice. There are striking parallels between orthomyxo- and nidovirus biology. Reminiscent of antigenic shifts in orthomyxoviruses, rodent coronaviruses exchanged S and HE sequences through recombination to extents not appreciated before. As for orthomyxovirus reassortants, the fitness of nidovirus recombinant offspring probably depends both on antigenic properties and on compatibility of receptor-binding and receptor-destroying activities.

Received for publication, August 23, 2004 , and in revised form, October 26, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY771998.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains an additional figure.

^¶ Supported by Netherlands Digestive Disease Foundation Project WS98-41.

^** Supported by the Academic Biomedical Center, Utrecht University (Expertise Center for Carbohydrate Analysis and Synthesis).

^¶¶ Supported by the Austrian Science Fund, Project P14104-MED.

^|||| To whom correspondence should be addressed. Tel.: 31-30-2531463/2485; Fax: 31-30-2536723; E-mail: R.Groot{at}vet.uu.nl.

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