Xylella fastidiosa disturbs nitrogen metabolism and causes a stress response in sweet orange Citrus sinensis cv. Pêra
Identifieur interne : 002507 ( Main/Merge ); précédent : 002506; suivant : 002508Xylella fastidiosa disturbs nitrogen metabolism and causes a stress response in sweet orange Citrus sinensis cv. Pêra
Auteurs : Rubia P. Purcino [Brésil] ; Camilo Lazaro Medina [Brésil] ; Daniel Martins [Brésil] ; Flavia Vischi Winck [Brésil] ; Eduardo Caruso Machado [Brésil] ; José Camilo Novello [Brésil] ; Marcos Antonio Machado [Brésil] ; Paulo Mazzafera [Brésil]Source :
- Journal of experimental botany [ 0022-0957 ] ; 2007.
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Abstract
Xylella fastidiosa (Xf) is a fastidious bacterium that grows exclusively in the xylem of several important crop species, including grape and sweet orange (Citrus sinensis L. Osb.) causing Pierce disease and citrus variegated chlorosis (CVC), respectively. The aim of this work was to study the nitrogen metabolism of a highly susceptible variety of sweet orange cv. 'Pêra' (C. sinensis L. Osbeck) infected with Xf. Plants were artificially infected and maintained in the greenhouse until they have developed clear disease symptoms. The content of nitrogen compounds and enzymes of the nitrogen metabolism and proteases in the xylem sap and leaves of diseased (DP) and uninfected healthy (HP) plants was studied. The activity of nitrate reductase in leaves did not change in DP, however, the activity of glutamine synthetase was significantly higher in these leaves. Although amino acid concentration was slightly higher in the xylem sap of DP, the level dropped drastically in the leaves. The protein contents were lower in the sap and in leaves of DP. DP and HP showed the same amino acid profiles, but different proportions were observed among them, mainly for asparagine, glutamine, and arginine. The polyamine putrescine was found in high concentrations only in DP. Protease activity was higher in leaves of DP while, in the xylem sap, activity was detected only in DP. Bidimensional electrophoresis showed a marked change in the protein pattern in DP. Five differentially expressed proteins were identified (2 from HP and 3 from DP), but none showed similarity with the genomic (translated) and proteomic database of Xf, but do show similarity with the proteins thaumatin, mucin, peroxidase, ABC-transporter, and strictosidine synthase. These results showed that significant changes take place in the nitrogen metabolism of DP, probably as a response to the alterations in the absorption, assimilation and distribution of N in the plant.
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<series><title level="j" type="main">Journal of experimental botany</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aminoacid</term>
<term>Chlorosis</term>
<term>Citrus sinensis</term>
<term>Metabolism</term>
<term>Nitrate reductase</term>
<term>Peptidases</term>
<term>Polyamine</term>
<term>Stress</term>
<term>Xylem</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Métabolisme</term>
<term>Stress</term>
<term>Aminoacide</term>
<term>Chlorose</term>
<term>Nitrate reductase</term>
<term>Polyamine</term>
<term>Peptidases</term>
<term>Xylème</term>
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<front><div type="abstract" xml:lang="en">Xylella fastidiosa (Xf) is a fastidious bacterium that grows exclusively in the xylem of several important crop species, including grape and sweet orange (Citrus sinensis L. Osb.) causing Pierce disease and citrus variegated chlorosis (CVC), respectively. The aim of this work was to study the nitrogen metabolism of a highly susceptible variety of sweet orange cv. 'Pêra' (C. sinensis L. Osbeck) infected with Xf. Plants were artificially infected and maintained in the greenhouse until they have developed clear disease symptoms. The content of nitrogen compounds and enzymes of the nitrogen metabolism and proteases in the xylem sap and leaves of diseased (DP) and uninfected healthy (HP) plants was studied. The activity of nitrate reductase in leaves did not change in DP, however, the activity of glutamine synthetase was significantly higher in these leaves. Although amino acid concentration was slightly higher in the xylem sap of DP, the level dropped drastically in the leaves. The protein contents were lower in the sap and in leaves of DP. DP and HP showed the same amino acid profiles, but different proportions were observed among them, mainly for asparagine, glutamine, and arginine. The polyamine putrescine was found in high concentrations only in DP. Protease activity was higher in leaves of DP while, in the xylem sap, activity was detected only in DP. Bidimensional electrophoresis showed a marked change in the protein pattern in DP. Five differentially expressed proteins were identified (2 from HP and 3 from DP), but none showed similarity with the genomic (translated) and proteomic database of Xf, but do show similarity with the proteins thaumatin, mucin, peroxidase, ABC-transporter, and strictosidine synthase. These results showed that significant changes take place in the nitrogen metabolism of DP, probably as a response to the alterations in the absorption, assimilation and distribution of N in the plant.</div>
</front>
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<name sortKey="Camilo Novello, Jose" sort="Camilo Novello, Jose" uniqKey="Camilo Novello J" first="José" last="Camilo Novello">José Camilo Novello</name>
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<name sortKey="Machado, Marcos Antonio" sort="Machado, Marcos Antonio" uniqKey="Machado M" first="Marcos Antonio" last="Machado">Marcos Antonio Machado</name>
<name sortKey="Martins, Daniel" sort="Martins, Daniel" uniqKey="Martins D" first="Daniel" last="Martins">Daniel Martins</name>
<name sortKey="Mazzafera, Paulo" sort="Mazzafera, Paulo" uniqKey="Mazzafera P" first="Paulo" last="Mazzafera">Paulo Mazzafera</name>
<name sortKey="Medina, Camilo Lazaro" sort="Medina, Camilo Lazaro" uniqKey="Medina C" first="Camilo Lazaro" last="Medina">Camilo Lazaro Medina</name>
<name sortKey="Purcino, Rubia P" sort="Purcino, Rubia P" uniqKey="Purcino R" first="Rubia P." last="Purcino">Rubia P. Purcino</name>
<name sortKey="Vischi Winck, Flavia" sort="Vischi Winck, Flavia" uniqKey="Vischi Winck F" first="Flavia" last="Vischi Winck">Flavia Vischi Winck</name>
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