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A more recent version of this article appeared on February 16, 2001
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M006077200v1
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Papers In Press, published online ahead of print December 4, 2000
J. Biol. Chem, 10.1074/jbc.M006077200
Submitted on July 11, 2000
Revised on December 1, 2000
Accepted on December 4, 2000

Elimination of phosphorylation sites of semliki forest virus replicase protein nsP3

Helena Vihinen, Tero Ahola, Minna Tuittila, Andres Merits, and Leevi Kaariainen

Institute of Biotechnology, University of Helsinki, Helsinki 00014

Corresponding Author: helena.vihinen{at}helsinki.fi

nsP3 is one of the four RNA replicase subunits encoded by alphaviruses. The specific essential functions of nsP3 remain unknown, but it is known to be phosphorylated on serine and threonine residues. Here we have completed mapping of the individual phosphorylation sites on Semliki Forest virus nsP3 (482 aa) by point mutational analysis of threonine residues. This showed that threonines 344 and 345 represented the major threonine phosphorylation sites in nsP3. Experiments with deletion variants suggested that nsP3 itself had no kinase activity, instead it was likely to be phosphorylated by multiple cellular kinases. Phosphorylation was not necessary for the peripheral membrane association of nsP3, which was mediated by the amino terminal region preceding the phosphorylation sites. Two deletion variants of nsP3 with either reduced or undetectable phosphorylation were studied in the context of virus infection. Cells infected with mutant viruses produced close to wild type levels of infectious virions, however, the rate of viral RNA synthesis was significantly reduced in the mutants. A virus totally defective in nsP3 phosphorylation and exhibiting a decreased rate of RNA synthesis also exhibited greatly reduced pathogenicity in mice.


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