The apoplastic antioxidant system in Prunus : response to long-term plum pox virus infection

This work describes, for the first time, the changes taking place in the antioxidative system of the leaf apoplast in response to plum pox virus (PPV) in different Prunus species showing different susceptibilities to PPV. The presence of p-hydroxymercuribenzoic acid (pHMB)-sensitive ascorbate peroxi...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 57(2006), 14 vom: 01., Seite 3813-24
1. Verfasser: Diaz-Vivancos, P (VerfasserIn)
Weitere Verfasser: Rubio, M, Mesonero, V, Periago, P M, Barceló, A Ros, Martínez-Gómez, P, Hernández, J A
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Antioxidants Plant Proteins Hydrogen Peroxide BBX060AN9V Catechol Oxidase EC 1.10.3.1 Peroxidases EC 1.11.1.- mehr... NAD+ peroxidase EC 1.11.1.1 Ascorbate Peroxidases EC 1.11.1.11 Peroxidase EC 1.11.1.7 Superoxide Dismutase EC 1.15.1.1
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100 1 |a Diaz-Vivancos, P  |e verfasserin  |4 aut 
245 1 4 |a The apoplastic antioxidant system in Prunus  |b response to long-term plum pox virus infection 
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500 |a Date Revised 17.03.2022 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a This work describes, for the first time, the changes taking place in the antioxidative system of the leaf apoplast in response to plum pox virus (PPV) in different Prunus species showing different susceptibilities to PPV. The presence of p-hydroxymercuribenzoic acid (pHMB)-sensitive ascorbate peroxidase (APX) (class I APX) and pHMB-insensitive APX (class III APX), superoxide dismutase (SOD), peroxidase (POX), NADH-POX, and polyphenoloxidase (PPO) was described in the apoplast from both peach and apricot leaves. PPV infection produced different changes in the antioxidant system of the leaf apoplast from the Prunus species, depending on their susceptibility to the virus. In leaves of the very susceptible peach cultivar GF305, PPV brought about an increase in class I APX, POX, NADH-POX, and PPO activities. In the susceptible apricot cultivar Real Fino, PPV infection produced a decrease in apoplastic POX and SOD activities, whereas a strong increase in PPO was observed. However, in the resistant apricot cultivar Stark Early Orange, a rise in class I APX as well as a strong increase in POX and SOD activities was noticed in the apoplastic compartment. Long-term PPV infection produced an oxidative stress in the apoplastic space from apricot and peach plants, as observed by the increase in H2O2 contents in this compartment. However, this increase was much higher in the PPV-susceptible plants than in the resistant apricot cultivar. Only in the PPV-susceptible apricot and peach plants was the increase in apoplastic H2O2 levels accompanied by an increase in electrolyte leakage. No changes in the electrolyte leakage were observed in the PPV-inoculated resistant apricot leaves, although a 42% increase in the apoplastic H2O2 levels was produced. Two-dimensional electrophoresis analyses revealed that the majority of the polypeptides in the apoplastic fluid had isoelectric points in the range of pI 4-6. The identification of proteins using MALDI-TOF (matrix-assisted laser desorption/ionization-time of flight) and peptide mass fingerprinting analyses showed the induction of a thaumatin-like protein as well as the decrease of mandelonitrile lyase in peach apoplast due to PPV infection. However, most of the selected polypeptides showed no homology with known proteins. This fact emphasizes that, at least in Prunus, most of the functions of the apoplastic space remain unknown. It is concluded that long-term PPV infection produced an oxidative stress in the leaf apoplast, contributing to the deleterious effects produced by PPV infection in leaves of inoculated, susceptible Prunus plants 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Antioxidants  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Hydrogen Peroxide  |2 NLM 
650 7 |a BBX060AN9V  |2 NLM 
650 7 |a Catechol Oxidase  |2 NLM 
650 7 |a EC 1.10.3.1  |2 NLM 
650 7 |a Peroxidases  |2 NLM 
650 7 |a EC 1.11.1.-  |2 NLM 
650 7 |a NAD+ peroxidase  |2 NLM 
650 7 |a EC 1.11.1.1  |2 NLM 
650 7 |a Ascorbate Peroxidases  |2 NLM 
650 7 |a EC 1.11.1.11  |2 NLM 
650 7 |a Peroxidase  |2 NLM 
650 7 |a EC 1.11.1.7  |2 NLM 
650 7 |a Superoxide Dismutase  |2 NLM 
650 7 |a EC 1.15.1.1  |2 NLM 
700 1 |a Rubio, M  |e verfasserin  |4 aut 
700 1 |a Mesonero, V  |e verfasserin  |4 aut 
700 1 |a Periago, P M  |e verfasserin  |4 aut 
700 1 |a Barceló, A Ros  |e verfasserin  |4 aut 
700 1 |a Martínez-Gómez, P  |e verfasserin  |4 aut 
700 1 |a Hernández, J A  |e verfasserin  |4 aut 
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