Elodie Vandelle

Prof. Elodie Vandelle

Department of Biotechnology - University of Verona, Italy
orcid

Research Focus & Metrics

Academic Career Length

24Years (2003-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 July 2006 in Molecular Plant-Microbe Interactions®
Verified
Journal Article
Open access
AGAngela Garcia-Brugger
Angela Garcia-Brugger
OLOlivier Lamotte
Olivier Lamotte
EVElodie Vandelle
Elodie Vandelle
SBStéphane Bourque
Stéphane Bourque
DLDavid Lecourieux
David Lecourieux
APAlain Pugin
Alain Pugin
Plant pathogen attacks are perceived through pathogen-issued compounds or plant-derived molecules that elicit defense reactions. Despite the large variety of elicitors, general schemes for cellular elicitor signaling leading to plant resistance can be drawn. In this article, we review early signaling events that happen after elicitor perception, including reversible protein phosphorylations, changes in the activities of plasma membrane proteins, variations in free calcium concentrations in cytosol and nucleus, and production of nitric oxide and active oxygen species. These events occur within the first minutes to a few hours after elicitor perception. One specific elicitor transduction pathway can use a combination or a partial combination of such events which can differ in kinetics and intensity depending on the stimulus. The links between the signaling events allow amplification of the signal transduction and ensure specificity to get appropriate plant defense reactions. This review first describes the early events induced by cryptogein, an elici-tor of tobacco defense reactions, in order to give a general scheme for signal transduction that will be use as a thread to review signaling events monitored in different elicitor or plant models.

1 December 2007 in The Plant Cell
Verified
Journal Article
Open access
MRMaría C Romero-Puertas
María C Romero-Puertas
MLMiriam Laxa
Miriam Laxa
AMAlessandro Mattè
Alessandro Mattè
FZFederica Zaninotto
Federica Zaninotto
IFIris Finkemeier
Iris Finkemeier
MDMassimo Delledonne
Massimo Delledonne
Nitric oxide (NO) is a free radical product of cell metabolism that plays diverse and important roles in the regulation of cellular function. S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification for the transduction of NO bioactivity, but very little is known about its physiological functions in plants. We investigated the molecular mechanism for S-nitrosylation of peroxiredoxin II E (PrxII E) from Arabidopsis thaliana and found that this posttranslational modification inhibits the hydroperoxide-reducing peroxidase activity of PrxII E, thus revealing a novel regulatory mechanism for peroxiredoxins. Furthermore, we obtained biochemical and genetic evidence that PrxII E functions in detoxifying peroxynitrite (ONOO−), a potent oxidizing and nitrating species formed in a diffusion-limited reaction between NO and O2 − that can interfere with Tyr kinase signaling through the nitration of Tyr residues. S-Nitrosylation also inhibits the ONOO− detoxification activity of PrxII E, causing a dramatic increase of ONOO−-dependent nitrotyrosine residue formation. The same increase was observed in a prxII E mutant line after exposure to ONOO−, indicating that the PrxII E modulation of ONOO− bioactivity is biologically relevant. We conclude that NO regulates the effects of its own radicals through the S-nitrosylation of crucial components of the antioxidant defense system that function as common triggers for reactive oxygen species– and NO-mediated signaling events.

1 August 2009 in Current Opinion in Plant Biology
Verified
Journal Article
Closed access
MLMargit Leitner
Margit Leitner
EVElodie Vandelle
Elodie Vandelle
FGFrank Gaupels
Frank Gaupels
DBDiana Bellin
Diana Bellin
MDMassimo Delledonne
Massimo Delledonne

1 June 2003 in Molecular Plant-Microbe Interactions®
Verified
Journal Article
Open access
BPBenoit Poinssot
Benoit Poinssot
EVElodie Vandelle
Elodie Vandelle
MBMarc Bentéjac
Marc Bentéjac
MAMarielle Adrian
Marielle Adrian
CLCaroline Levis
Caroline Levis
APAlain Pugin
Alain Pugin
A purified glycoprotein from Botrytis cinerea(strain T4), identified as endopolygalacturonase 1 (T4BcPG1) by mass spectrometry analysis, has been shown to activate defense reactions in grapevine (Vitis vinifera cv. Gamay). These reactions include calcium influx, production of active oxygen species, activation of two mitogen-activated protein kinases, defense gene transcript accumulation, and phytoalexin production. Most of these defense reactions were also activated in grapevine in response to purified oligogalacturonides (OGA) with a degree of polymerization of 9 to 20. In vivo, these active OGA might be a part of the released products resulting from endopolygalacturonase activity on plant cell walls. Nevertheless, the intensity and kinetics of events triggered by OGA were very different when compared with T4BcPG1 effects. Moreover, chemical treatments of T4BcPG1 and desensitization assays have allowed us to discriminate enzymatic and elicitor activities, indicating that elicitor activity was not due to released oligogalacturonides. Thus, BcPG1 should be considered as both an avirulence and a virulence factor. The role of the secreted BcPG1 in the pathogenicity of Botrytis cinerea is discussed.

1 April 2006 in Molecular Plant-Microbe Interactions®
Verified
Journal Article
Open access
EVElodie Vandelle
Elodie Vandelle
BPBenoit Poinssot
Benoit Poinssot
DWDavid Wendehenne
David Wendehenne
MBMarc Bentéjac
Marc Bentéjac
APAlain Pugin
Alain Pugin
We have already reported the identification of the endopolygalacturonase 1 (BcPG1) from Botrytis cinerea as a potent elicitor of defense responses in grapevine, independently of its enzymatic activity. The aim of the present study is the analysis of the signaling pathways triggered by BcPG1 in grapevine cells. Our data indicate that BcPG1 induces a Ca2+ entry from the apoplasm, which triggers a phosphorylation-dependent nitric oxide (NO) production via an enzyme probably related to a NO synthase. Then NO is involved in i) cytosolic calcium homeostasis, by activating Ca2+ release from internal stores and regulating Ca2+ fluxes across the plasma membrane, ii) plasma membrane potential variation, iii) the activation of active oxygen species (AOS) production, and iv) defense gene expression, including phenylalanine ammonia lyase and stilbene synthase, which encode enzymes responsible for phytoalexin biosynthesis. Interestingly enough, mitogen-activated protein kinase (MAPK) activation is independent of this regulation pathway that closely connects Ca2+, NO, and AOS.

1 November 2011 in Plant Science
Verified
Journal Article
Closed access
EVElodie Vandelle
Elodie Vandelle
MDMassimo Delledonne
Massimo Delledonne