Open AccessPotato virus X movement in Nicotiana benthamiana : new details revealed by chimeric coat protein variants
Author(s) -
BETTI CAMILLA,
LICO CHIARA,
MAFFI DARIO,
D'ANGELI SIMONE,
ALTAMURA MARIA MADDALENA,
BENVENUTO EUGENIO,
FAORO FRANCO,
BASCHIERI SELENE
Publication year - 2012
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1111/j.1364-3703.2011.00739.x
Subject(s) - nicotiana benthamiana , biology , movement protein , potato virus x , microbiology and biotechnology , mutant , virus , fusion protein , coat protein , plant virus , virology , phloem , capsid , recombinant dna , biochemistry , gene , rna , botany
SUMMARY Potato virus X coat protein is necessary for both cell‐to‐cell and phloem transfer, but it has not been clarified definitively whether it is needed in both movement phases solely as a component of the assembled particles or also of differently structured ribonucleoprotein complexes. To clarify this issue, we studied the infection progression of a mutant carrying an N‐terminal deletion of the coat protein, which was used to construct chimeric virus particles displaying peptides selectively affecting phloem transfer or cell‐to‐cell movement. Nicotiana benthamiana plants inoculated with expression vectors encoding the wild‐type, mutant and chimeric viral genomes were examined by microscopy techniques. These experiments showed that coat protein–peptide fusions promoting cell‐to‐cell transfer only were not competent for virion assembly, whereas long‐distance movement was possible only for coat proteins compatible with virus particle formation. Moreover, the ability of the assembled PVX to enter and persist into developing xylem elements was revealed here for the first time.