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Journal of Virology, January 2006, p. 1053-1058, Vol. 80, No. 2
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.2.1053-1058.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

ATP Hydrolysis and AMP Kinase Activities of Nonstructural Protein 2C of Human Parechovirus 1

Department of Virology, Haartman Institute, University of Helsinki, FIN-00014 Helsinki, Finland,¹ Institute of Biotechnology, University of Helsinki, FIN-00014 Helsinki, Finland,² Department of Virology, University of Turku, FIN-20520 Turku, Finland³

Received 26 July 2005/ Accepted 19 October 2005

The highly conserved picornavirus 2C proteins, thought to be involved in genome replication, contain three motifs found in NTPases/helicases of superfamily III. We report that human parechovirus 1 2C displays Mg²⁺-dependent ATP diphosphohydrolase activity in vitro, whereas other nucleoside triphosphates are not substrates for the hydrolysis. We also found that the 2C protein has an enzymatic activity that converts AMP to a corresponding diphosphate using ADP or ATP as a phosphate donor. In addition, we observed that ATP hydrolysis results in 2C autophosphorylation. These findings indicate that the parechovirus 2C protein has enzymatic activities, which may contribute to several functions in the viral replication cycle.

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