Affinity purification and characterization of a binding protein for a hepta-β-glucoside. Phytoalexin elicitor in soybean

Frey, Thomas; Cosio, Eric G.; Ebel, Jorgen

doi:10.1016/s0031-9422(00)95134-3

Cited by 51 publications

(44 citation statements)

References 20 publications

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“…However, eluates from the ␤-glucan matrix did not only contain the 75-kDa protein. Other, less abundant protein species with molecular masses of approximately 100 and 33 kDa were observed in slightly different experimental conditions (19,46). Because of the similarity of kinetic data between the native and the recombinant protein (Table III) we conclude that at least the major portion of the enzyme activity in the eluate from the affinity column is based on the native GBP.…”

Section: Table I Comparison Of Specific Binding and Biological Activimentioning

confidence: 78%

An Ancient Enzyme Domain Hidden in the Putative β-Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance

Fliegmann

Mithöfer

Wanner

et al. 2004

Journal of Biological Chemistry

142

113

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A successful defense against potential pathogens requires that a host organism is able to discriminate between self and nonself structures. Soybean (Glycine max L.) exploits a specific molecular pattern, a 1,6-␤-linked and 1,3-␤-branched heptaglucoside (HG), present in cell walls of the oomycetal pathogen Phytophthora sojae, as a signal compound eliciting the onset of defense reactions. The specific and high affinity HG-binding site is contained in the ␤-glucan-binding protein (GBP), which in turn is part of a proposed receptor complex. The ability to perceive and respond to Phytophthora cell wall-derived ␤-glucan elicitors is exclusive to plants that belong to the Fabaceae. However, we propose that the presence of the GBP is essential, but not sufficient for ␤-glucan elicitor-dependent disease resistance because genes encoding GBP-related proteins can be retrieved from many plant species. Furthermore, we show that the GBP is composed of two different carbohydrateactive protein domains, one containing the ␤-glucanbinding site, and the other related to glucan endoglucosidases of fungal origin. The glucan hydrolase displays most likely an endo-specific mode of action, cleaving only 1,3-␤-D-glucosidic linkages of oligoglucosides consisting of at least four moieties. Thus, the intrinsic endo-1,3-␤-glucanase activity of the GBP is perfectly suited during initial contact with Phytophthora to release oligoglucoside fragments enriched in motifs that constitute ligands for the high affinity binding site present in the same protein. The concept of innate immunity in plants receives substantial support by this highly sophisticated system using ancient enzyme modules as an active part of the recognition mechanism.

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Section: Table I Comparison Of Specific Binding and Biological Activimentioning

confidence: 78%

An Ancient Enzyme Domain Hidden in the Putative β-Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance

Fliegmann

Mithöfer

Wanner

et al. 2004

Journal of Biological Chemistry

142

113

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“…Although it has been partially purified and characterized (Ayers et al, 1976a(Ayers et al, , 1976b, it has not been subjected to acidic (Ayers et al, 1976b;Sharp et al, 1984) or enzymatic (Cline and Albersheim, 1981;Keen and Yoshikawa, 1983;Ham, et al, 1991) hydrolysis or fractionation. Acid-released fragments have been purified and synthesized accordingly and are being used to characterize glucan-binding activities in soybean plasma membranes (Cheong and Hahn, 1991;Frey et al, 1993). A binding activity for enzymatically released glucan fragments has also been characterized (Yoshikawa and Sugimoto, 1993).…”

Section: I Scu Sslo N Separation Of Individual Responses To Primarymentioning

confidence: 99%

Signaling in Soybean Phenylpropanoid Responses (Dissection of Primary, Secondary, and Conditioning Effects of Light, Wounding, and Elicitor Treatments)

Graham

1996

Plant Physiol.

123

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“…Two groups have previously reported apparent dissociation constants of 1 nM (20) (1997) values which are of the same order of magnitude as those of the present study. Recently, a photoaffinity labeling technique and affinity chromatography have been used to demonstrate that 70-, 100-, and 170-kDa polypeptides have binding activity (41,42). We obtained preliminary data indicating that hepta-␤-glucoside could partially inhibit glucan-binding activity against the recombinant protein by 51% (data not shown).…”

Section: Discussionmentioning

confidence: 86%

The structure and function of a soybean β-glucan-elicitor-binding protein

Umemoto

Kakitani

Iwamatsu

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

214

118

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ABSTRACT␤-Glucan elicitor (GE), released from the cell wall of the phytopathogenic fungus Phytophthora megasperma by soybean glucanases, causes defense reactions in soybean. A GE-binding protein (GEBP) was purified from the membrane fraction of soybean root cells, and its cDNA was isolated. Expression of the cDNA clone in tobacco suspension cultured cells and in Escherichia coli conferred GE-binding activity to both. An antibody against the recombinant protein was found to inhibit the GE binding with the soybean cotyledon membrane fraction as well as the resulting accumulation of phytoalexin. Immunolocalization assays indicated that the GEBPs are located in the plasma membrane of root cells. These results suggest that the cDNA encodes a GE receptor and may mediate the signaling of the elicitor.Plants defend themselves from infection by invasive phytopathogenic fungi by a combination of constitutive as well as induced defenses such as phytoalexin accumulation; the hypersensitive reaction; and the production of chitinase, glucanase, and polygalacturonase inhibitor (1). Certain defense reactions are elicited by compounds referred to as elicitors, such as oligosaccharides, proteins, and glycoproteins released from fungal and plant cell walls (reviewed in refs. 2-4).

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Affinity purification and characterization of a binding protein for a hepta-β-glucoside. Phytoalexin elicitor in soybean

Cited by 51 publications

References 20 publications

An Ancient Enzyme Domain Hidden in the Putative β-Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance

An Ancient Enzyme Domain Hidden in the Putative β-Glucan Elicitor Receptor of Soybean May Play an Active Part in the Perception of Pathogen-associated Molecular Patterns during Broad Host Resistance

Signaling in Soybean Phenylpropanoid Responses (Dissection of Primary, Secondary, and Conditioning Effects of Light, Wounding, and Elicitor Treatments)

The structure and function of a soybean β-glucan-elicitor-binding protein

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