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Journal of Virology, July 2004, p. 7833-7838, Vol. 78, No. 14
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.14.7833-7838.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Human Coronavirus 229E Nonstructural Protein 13: Characterization of Duplex-Unwinding, Nucleoside Triphosphatase, and RNA 5'-Triphosphatase Activities

Konstantin A. Ivanov and John Ziebuhr*

Institute of Virology and Immunology, University of Würzburg, Würzburg, Germany

Received 14 January 2004/ Accepted 16 March 2004

The human coronavirus 229E (HCoV-229E) replicase gene-encoded nonstructural protein 13 (nsp13) contains an N-terminal zinc-binding domain and a C-terminal superfamily 1 helicase domain. A histidine-tagged form of nsp13, which was expressed in insect cells and purified, is reported to unwind efficiently both partial-duplex RNA and DNA of up to several hundred base pairs. Characterization of the nsp13-associated nucleoside triphosphatase (NTPase) activities revealed that all natural ribonucleotides and nucleotides are substrates of nsp13, with ATP, dATP, and GTP being hydrolyzed most efficiently. Using the NTPase active site, HCoV-229E nsp13 also mediates RNA 5'-triphosphatase activity, which may be involved in the capping of viral RNAs.

* Corresponding author. Mailing address: Institute of Virology and Immunology, University of Würzburg, Versbacher Str. 7, Würzburg 97078, Germany. Phone: 49-931-20149928. Fax: 49-931-20149553. E-mail: j.ziebuhr{at}mail.uni-wuerzburg.de.

Journal of Virology, July 2004, p. 7833-7838, Vol. 78, No. 14
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.14.7833-7838.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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Copyright © 2004 by the American Society for Microbiology. All rights reserved.