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Journal of Virology, November 2000, p. 10846-10851, Vol. 74, No. 22
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

ATP Binding and ATPase Activities Associated with Recombinant Rabbit Hemorrhagic Disease Virus 2C-Like Polypeptide

M. Soledad Marín, Rosa Casais, José M. Martín Alonso, and Francisco Parra*

Departamento de Bioquímica y Biología Molecular, Instituto Universitario de Biotecnología de Asturias (CSIC), Universidad de Oviedo, 33006 Oviedo, Spain

Received 27 January 2000/Accepted 16 August 2000

The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 polyprotein cleavage product has been expressed in Escherichia coli as a glutathione S-transferase (GST) fusion protein. The recombinant GST-Delta 2C protein showed in vitro ATP-binding and ATPase activities. Site-directed mutagenesis studies of the conserved residues G522 and T529 in motif A, D566 and E567 in motif B, and K600 in motif C were also performed. These results provide the first experimental characterization of a 2C-like ATPase activity in a member of the Caliciviridae.

* Corresponding author. Mailing address: Departamento de Bioquímica y Biología Molecular, Universidad de Oviedo, 33006 Oviedo, Spain. Phone: 34-985103563. Fax: 34-985103157. E-mail: parra{at}biosun.medicina.uniovi.es.

Journal of Virology, November 2000, p. 10846-10851, Vol. 74, No. 22
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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