An ancient enzyme domain hidden in the putative beta-glucan elicitor receptor of soybean may play an active part in the perception of pathogen-associated molecular patterns during broad host resistance.
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-beta-linked and 1,3-beta-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 beta-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 beta-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 beta-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 beta-glucan-binding 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-beta-d-glucosidic linkages of oligoglucosides consisting of at least four moieties. Thus, the intrinsic endo-1,3-beta-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.
Department Biologie I/Botanik, Ludwig-Maximilians Universität, Menzinger Str. 67, D-80638 München, Germany. judith.fliegmann@lmu.de
Judith
J
Fliegmann
Axel
A
Mithofer
Gerhard
G
Wanner
Jurgen
J
Ebel
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D015153:Blotting, Western; D002241:Carbohydrates / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D002460:Cell Line; D002473:Cell Wall / Q000737:chemistry; D018076:DNA, Complementary / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D005936:Glucans / Q000378:metabolism; D005960:Glucosides / Q000737:chemistry; D007150:Immunohistochemistry; D007313:Insecta; D007700:Kinetics; D037102:Lectins; D008024:Ligands; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009154:Mutation; D010838:Phytophthora / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000378:metabolism*; D013997:Time Factors
D002241:Carbohydrates; D002352:Carrier Proteins; D018076:DNA, Complementary; D005936:Glucans; D005960:Glucosides; D037102:Lectins; D008024:Ligands; D011994:Recombinant Proteins; C037937:glucan-binding proteins