Constitutive cyclic GMP accumulation in Arabidopsis thaliana compromises systemic acquired resistance induced by an avirulent pathogen by modulating local signals.
The infection of Arabidopsis thaliana plants with avirulent pathogens causes the accumulation of cGMP with a biphasic profile downstream of nitric oxide signalling. However, plant enzymes that modulate cGMP levels have yet to be identified, so we generated transgenic A. thaliana plants expressing the rat soluble guanylate cyclase (GC) to increase genetically the level of cGMP and to study the function of cGMP in plant defence responses. Once confirmed that cGMP levels were higher in the GC transgenic lines than in wild-type controls, the GC transgenic plants were then challenged with bacterial pathogens and their defence responses were characterized. Although local resistance was similar in the GC transgenic and wild-type lines, differences in the redox state suggested potential cross-talk between cGMP and the glutathione redox system. Furthermore, large-scale transcriptomic and proteomic analysis highlighted the significant modulation of both gene expression and protein abundance at the infection site, inhibiting the establishment of systemic acquired resistance. Our data indicate that cGMP plays a key role in local responses controlling the induction of systemic acquired resistance in plants challenged with avirulent pathogens.
Department of Biotechnology, University of Verona, Verona, Italy.
Jamshaid
J
Hussain
Department of Biotechnology, University of Verona, Verona, Italy.
Jian
J
Chen
Unit of Food Science and Nutrition, Department of Medicine, University Campus Bio-Medico of Rome, Rome, Italy.
Vittoria
V
Locato
Institute of Biosciences and Bioresources - National Research Council, Bari, Italy.
Wilma
W
Sabetta
Department of Biosciences, University of Milan, Milan, Italy.
Smrutisanjita
S
Behera
Unit of Food Science and Nutrition, Department of Medicine, University Campus Bio-Medico of Rome, Rome, Italy.
Sara
S
Cimini
Department of Biotechnology, University of Verona, Verona, Italy.
Francesca
F
Griggio
Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm, Germany.
Silvia
S
Martínez-Jaime
Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm, Germany.
Alexander
A
Graf
Department of Biotechnology, University of Verona, Verona, Italy.
Mabrouk
M
Bouneb
Department of Biotechnology, University of Verona, Verona, Italy.
Raman
R
Pachaiappan
Unit of Food Science and Nutrition, Department of Medicine, University Campus Bio-Medico of Rome, Rome, Italy.
Paola
P
Fincato
Institute of Biosciences and Bioresources - National Research Council, Bari, Italy.
Emanuela
E
Blanco
Department of Biosciences, University of Milan, Milan, Italy.
Alex
A
Costa
Unit of Food Science and Nutrition, Department of Medicine, University Campus Bio-Medico of Rome, Rome, Italy.
Laura
L
De Gara
Department of Biotechnology, University of Verona, Verona, Italy.
Diana
D
Bellin
Department of Biology, University of Bari "Aldo Moro", Bari, Italy.
Maria Concetta
MC
de Pinto
Department of Biotechnology, University of Verona, Verona, Italy.
Elodie
E
Vandelle
D000818:Animals; D017360:Arabidopsis / Q000378:metabolism*; D001205:Ascorbic Acid / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D006152:Cyclic GMP / Q000378:metabolism*; D060467:Disease Resistance / Q000502:physiology*; D018506:Gene Expression Regulation, Plant; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism; D006162:Guanylate Cyclase / Q000235:genetics / Q000378:metabolism*; D018515:Plant Leaves / Q000378:metabolism; D030821:Plants, Genetically Modified / Q000378:metabolism; D020543:Proteome / Q000378:metabolism; D044224:Pseudomonas syringae / Q000235:genetics / Q000472:pathogenicity; D051381:Rats; D059467:Transcriptome
C100931:AvrB protein, Pseudomonas syringae; D001426:Bacterial Proteins; D020543:Proteome; D006162:Guanylate Cyclase; D005978:Glutathione; D006152:Cyclic GMP; D001205:Ascorbic Acid