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Virology. 1998 Sep 1;248(2):323-31.

Deletions in the conserved amino-terminal basic arm of cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement.

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Department of Plant Pathology, University of California, Riverside, California, 92521-0122, USA.


The N-terminal basic arm of cucumber mosaic cucumovirus (CMV) coat protein (CP) contains a conserved arginine-rich motif, which is characteristic of RNA binding proteins of several plant and nonplant viruses. To identify regions of the CMV CP N-terminus that are essential for interacting with viral genomic RNA, a comprehensive set of mutations was engineered into biologically active clones of CMV RNA3 and the behavior of each variant with respect to infectivity, packaging and movement was examined. Biological assays conducted in Chenopodium quinoa (local lesion host) and Nicotiana benthamiana (systemic host) revealed that variants lacking either 12 N-proximal amino acids or a region containing four consecutive arginine residues of the CP N-terminus were competent for assembly into virions and remained infectious in plants. Interestingly, two other variants, lacking either 19 N-proximal amino acids or a domain containing a cluster of six arginines in the arginine-rich motif, were incompetent for virion assembly but retained the ability to move cell to cell. Taken together, these results indicate that a major portion of the N-terminal basic arm of CMV CP is dispensable for CP-RNA interactions and also establish that CMV can move cell to cell in a nonvirion form. The distinctive role played by the viral CP in movement and specifically, the extent to which the CP N-terminal basic arm is involved in the infection cycle of CMV are discussed.

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