Mutational analysis of the cowpea mosaic virus movement protein.

P Bertens, J Wellink, R Goldbach, A van Kammen

Journal: Virology 2000;267(2):199-208

PMID: 10662615

Abstract

Cowpea mosaic virus moves from cell-to-cell in a virion form through tubular structures that are assembled in modified plasmodesmata. Similar tubular structures are formed on the surface of protoplasts inoculated with cowpea mosaic virus. The RNA 2-encoded movement protein (MP) is responsible for the induction and formation of these structures. To define functional domains of the MP, an alanine-substitution mutagenesis was performed on eight positions in the MP, including two conserved sequence motifs, the LPL and D motifs. Results show that these two conserved motifs as well as the central region of the MP are essential for cell-to-cell movement. Several viruses carrying mutations in the N- or C-terminal parts of their MP retained infectivity on cowpea plants. Coexpression studies revealed that mutant MPs did not interfere with the activity of wild-type MP and could not mutually complement their defects.

Copyright 2000 Academic Press.

Address: Laboratories of Molecular Biology, Virology, Graduate School for Experimental Plant Sciences, Wageningen University, Dreijenlaan 3, Wageningen, 6703 HA, The Netherlands.
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