conference schedule and program with abstracts - Horticulture ...
conference schedule and program with abstracts - Horticulture ...
conference schedule and program with abstracts - Horticulture ...
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P-40<br />
Towards a characterization of the PR-10 gene family in grapevine<br />
M. Aless<strong>and</strong>rini, L. Bortesi, A. Lovato, M. Fasoli, G. Zoccatelli, S. Zenoni, V. Trope, M.<br />
Pezzotti, A. Polverari*<br />
Dipartimento di Biotecnologie, Università di Verona, Verona, Italy<br />
*Corresponding author: annalisa.polverari@univr.it<br />
We have started a project aimed at characterizing the expression profile <strong>and</strong> protein activity<br />
of pathogenesis related proteins of the PR-10 family in grapevine. According to a large scale<br />
microarray analysis carried out on a Combimatrix grapevine chip, the expression of several<br />
Tentative consensus annotated as similar to PR-10 proteins is strongly increased in resistant<br />
Vitis riparia, <strong>and</strong> to a lesser extent in V. vinifera, following infection <strong>with</strong> Plasmopara<br />
viticola (Polesani et al., BMC Genomics 2010). PR-10 proteins are induced by pathogen<br />
infection <strong>and</strong> abiotic stresses in a number of species; because they often show<br />
ribonucleolytic activity it has been suggested that they may be involved in antiviral defence;<br />
their antimicrobial activity has been tested <strong>with</strong> controversial results. Up to now, we have<br />
analyzed the expression level of four members of the PR-10 family, predicted in the Vitis<br />
vinifera genome, by Real-time RT-PCR, in response to P. viticola infection at 12 <strong>and</strong> 24<br />
hours post-inoculation (hpi). All are barely detectable in healthy V. vinifera leaves but are<br />
induced, <strong>with</strong> similar levels, in response to infection. An homologous gene, that we called<br />
Vr-PR10, has been isolated from the resistant species Vitis riparia following infection; its<br />
coding sequence has been cloned from V. riparia cDNA <strong>and</strong> the corresponding protein<br />
expressed in E. coli. The purified protein showed ribonucleolytic activity in vitro. Using<br />
antibodies raised against the recombinant protein, which recognize the native protein from<br />
leaf tissue in Western blot analyses, a strong induction of the protein upon infection was<br />
shown. The protein is now being tested for antimicrobial <strong>and</strong> antiviral activity in vitro <strong>and</strong><br />
in vivo.<br />
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