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Journal of Virology, March 2006, p. 3108-3111, Vol. 80, No. 6
0022-538X/06/$08.00+0 doi:10.1128/JVI.80.6.3108-3111.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Program in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, Helsinki, Finland,1 Estonian Biocentre and Institute of Molecular and Cellular Biology, Tartu, Estonia2
Received 7 September 2005/ Accepted 21 December 2005
We have sequenced the nonstructural protein coding region of Semliki Forest virus temperature-sensitive (ts) mutant strains ts1, ts6, ts9, ts10, ts11, ts13, and ts14. In each case, the individual amino acid changes uncovered were transferred to the prototype strain background and thereby identified as the underlying cause of the altered RNA synthesis phenotype. All mutations mapping to the protease domain of nonstructural protein nsP2 caused defects in nonstructural polyprotein processing and subgenomic RNA synthesis, and all mutations in the helicase domain of nsP2 affected subgenomic RNA production. These types of defects were not associated with mutations in other nonstructural proteins.
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