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Journal of General Virology (2000), 81, 1961-1965.
© 2000 Society for General Microbiology

Animal: RNA Viruses

NTP binding and phosphohydrolase activity associated with purified bluetongue virus non-structural protein NS2

Nigel J. Horscroftb,1,2 and Polly Roy1,2,3

Department of Biochemistry, Oxford University, Oxford OX1 3QU, UK1
NERC Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR, UK2
Department of Geographic Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA3

Author for correspondence: Polly Roy (at NERC Institute of Virology and Environmental Microbiology). Fax +44 1865 281696. e-mail por{at}wpo.nerc.ac.uk

The bluetongue virus ssRNA-binding protein, NS2, is a phosphoprotein that forms viral inclusion bodies in infected cells. Recombinant NS2 was expressed in the baculovirus expression system and purified to homogeneity from insect cells. Purified NS2 bound nucleosides. Further investigation revealed that the protein bound ATP and GTP and could hydrolyse both nucleosides to their corresponding NMPs, with a higher efficiency for the hydrolysis of ATP. The increased efficiency of hydrolysis of ATP correlated with a higher binding affinity of NS2 for ATP than GTP. Ca2+, Mg2+ and Mn2+ were able to function as the required divalent cation in the reactions. The phosphohydrolase activity was not sensitive to ouabain, an inhibitor of cellular ATPases, suggesting that this activity was not the result of a cellular contaminant.




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