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  Elicitor-binding proteins and signal transduction in the activation of a phytoalexin defense response

Ebel, J., Bhagwat, A. A., Cosio, E. G., Feger, M., Kissel, U., Mithöfer, A., et al. (1995). Elicitor-binding proteins and signal transduction in the activation of a phytoalexin defense response. Canadian Journal of Botany, 73, 506-510. doi:10.1139/b95-289.

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 Urheber:
Ebel, J., Autor
Bhagwat, A. A., Autor
Cosio, E. G., Autor
Feger, M., Autor
Kissel, U., Autor
Mithöfer, Axel1, Autor           
Waldmüller, T., Autor
Affiliations:
1External Organizations, ou_persistent22              

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Schlagwörter: soybean (glycine max) phytophthora megasperma f sp glycinea beta-glucan elicitor elicitor-binding proteins phytoalexins ca2+ host-pathogen interactions high-affinity binding soybean glycine-max f-sp glycinea mycelial walls var sojae glucan fractions bradyrhizobium purification
 Zusammenfassung: Inducible plant defenses against potential pathogens are thought to be activated by signal compounds released during early stages of the infection process. In the incompatible interaction between soybean (Glycine max L.) and the oomycete Phytophthora megasperma f.sp. glycinea (= Phytophthora sojae) a rapid, localized phytoalexin response is activated at the level of transcription. The phytoalexin response is also stimulated in various soybean tissues, including cultured cells, following treatment with an elicitor derived from the cell walls of the fungus. The best characterized elicitors of P. megasperma for soybean are the branched (1-->3)- and (1-->6)-linked beta-glucans, structural polysaccharides of the hyphal waifs. The glucans are naturally released during the early stages of germination of the fungal cysts in a host-independent manner. Cyclic beta-glucans of Bradyrhizobium japonicum USDA 110, a symbiont of soybean, are not active in inducing phytoalexin production in soybean. When tested in combination, B. japonicum beta-glucans inhibited stimulation of phytoalexin accumulation by the fungal glucans. Surface-localized glucan-binding proteins exist in soybean cells that display high affinity and specificity for the fungal beta-glucans, including an elicitor-active hepta-beta-glucoside fragment derived from the polysaccharide, suggesting that elicitor action involves a transmembrane signalling process. The main component of the soybean beta-glucan binding sites appears to be a 70-kDa protein. Hepta-beta-glucoside binding sites exist in several other legumes, such as bean (Phaseolus vulgaris L.), pea (Pisum sativum L.), and lupine (Lupinus albus L.). The signalling process initiated by the beta-glucan elicitor, which leads to the activation of the phytoalexin defense response in soybean, involves changes in the permeability of the plasma membrane to Ca2+ and H+. Chloride channel antagonists are more efficient than calcium channel antagonists in inhibiting both the phytoalexin response and the inducible ion fluxes. The results present evidence that the observed permeability changes of the plasma membrane are primary events in the transduction of the elicitor signal(s) by the challenged soybean cells.

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 Datum: 1995
 Publikationsstatus: Erschienen
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 Identifikatoren: Anderer: EXT048
DOI: 10.1139/b95-289
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Titel: Canadian Journal of Botany
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Ottawa : NRC Research Press
Seiten: - Band / Heft: 73 Artikelnummer: - Start- / Endseite: 506 - 510 Identifikator: ISSN: 0008-4026
CoNE: https://pure.mpg.de/cone/journals/resource/110992357320146