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Journal of Virology, January 2003, p. 1452-1461, Vol. 77, No. 2
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.2.1452-1461.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Yoshimi Okada,1 and Yuichiro Watanabe1*
Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902,1 Faculty of Agriculture, Tokyo University of Agriculture and Engineering, Tokyo 183-0054, Japan,3 Donald Danforth Plant Science Center, St. Louis, Missouri 631322
Received 6 May 2002/ Accepted 4 October 2002
We reported previously that the movement protein (MP) of tomato mosaic tobamovirus is phosphorylated, and we proposed that MP phosphorylation is important for viral pathogenesis. Experimental data indicated that phosphorylation enhances the stability of MP in vivo and enables the protein to assume the correct intracellular location to perform its function. A mutant virus designated 37A238A was constructed; this virus lacked two serine residues within the MP, which prevented its phosphorylation. In the present study, we inoculated plants with the 37A238A mutant, and as expected, it was unable to produce local lesions on the leaves. However, after an extended period, we found that lesions did occur, which were due to revertant viruses. Several revertants were isolated, and the genetic changes in their MPs were examined together with any changes in their in vivo characteristics. We found that reversion to virulence was associated first with increased MP stability in infected cells and second with a shift in MP intracellular localization over time. In one case, the revertant MP was not phosphorylated in vivo, but it was functional.
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