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Journal of Virology, October 2000, p. 9586-9593, Vol. 74, No. 20
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Biochemical Characterization of the Equine Arteritis Virus Helicase Suggests a Close Functional Relationship between Arterivirus and Coronavirus Helicases

Anja Seybert,1 Leonie C. van Dinten,2,dagger Eric J. Snijder,2 and John Ziebuhr1,*

Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany,1 and Department of Virology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, The Netherlands2

Received 15 June 2000/Accepted 18 July 2000

The arterivirus equine arteritis virus nonstructural protein 10 (nsp10) has previously been predicted to contain a Zn finger structure linked to a superfamily 1 (SF1) helicase domain. A recombinant form of nsp10, MBP-nsp10, was produced in Escherichia coli as a fusion protein with the maltose-binding protein. The protein was partially purified by affinity chromatography and shown to have ATPase activity that was strongly stimulated by poly(dT), poly(U), and poly(dA) but not by poly(G). The protein also had both RNA and DNA duplex-unwinding activities that required the presence of 5' single-stranded regions on the partial-duplex substrates, indicating a 5'-to-3' polarity in the unwinding reaction. Results of this study suggest a close functional relationship between the arterivirus nsp10 and the coronavirus helicase, for which NTPase and duplex-unwinding activities were recently demonstrated. In a number of biochemical properties, both arterivirus and coronavirus SF1 helicases differ significantly from the previously characterized RNA virus SF1 and SF2 enzymes. Thus, the combined data strongly support the idea that nidovirus helicases may represent a separate group of RNA virus-encoded helicases with distinct properties.

* Corresponding author. Mailing address: Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, 97078 Würzburg, Germany. Phone: 49-931-2013966. Fax: 49-931-2013934. E-mail: ziebuhr{at}vim.uni-wuerzburg.de.

dagger Present address: Department of Molecular Virology, Institut Jacques-Monod, 75251 Paris Cedex 05, France.

Journal of Virology, October 2000, p. 9586-9593, Vol. 74, No. 20
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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