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Potential Involvement of a Cucumber Homolog of Phloem Protein 1 in the Long-Distance Movement of Cucumber mosaic virus Particles

July 2006 , Volume 19 , Number  7
Pages  734 - 746

A. Requena , L. Simón-Buela , G. Salcedo , and F. García-Arenal

Dpto. Biotecnología, ETSI. Agrónomos, Universidad Politécnica de Madrid, Avda. Complutense s/n, 28040 Madrid, Spain


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Accepted 28 February 2006.

The systemic movement of Cucumber mosaic virus (CMV) in cucumber plants was analyzed. The structure that is translocated and its putative interactions with phloem components were analyzed in phloem exudate (PE) samples, which reflect sieve tubes stream composition. Rate zonal centrifugation and electron-microscopy analyses of PE from CMV-infected plants showed that CMV moves through sieve tubes as virus particles. Gel overlay assays revealed that CMV particles interact with a PE protein, p48. The amino-acid sequence of several tryptic peptides of p48 was determined. Partial amino-acid sequence of p48 showed it was a cucumber homolog of phloem protein 1 (PP1) from pumpkin, with which p48 also shares several chemical properties. PP1 from pumpkin has plasmodes-mata-gating ability and translocates in sieve tubes. Encapsidated CMV RNA in PE samples from infected plants was less accessible to digestion by RNase A than RNA in purified CMV particles, a property that was reconstituted by the in vitro interaction of purified CMV particles and protein p48. These results indicate that the interaction with p48 modifies CMV particle structure and suggest that CMV particles interact with the cucumber homolog of PP1 during translocation in the sieve tubes.


Additional keywords: phloem proteins , phloem transport .

© 2006 The American Phytopathological Society