Search

The cytokinin signaling pathway, which is mediated by Arabidopsis response regulator (ARR) proteins, has been involved in the modulation of some disease-resistance responses. Here, we describe novel functions of ARR6 in the control of plant disease-resistance and cell-wall composition. Plants impaired in ARR6 function (arr6) were more resistant and susceptible, respectively, to the necrotrophic fungus Plectosphaerella cucumerina and to the vascular bacterium Ralstonia solanacearum, whereas Arabidopsis plants that overexpress ARR6 showed the opposite phenotypes, which further support a role of ARR6 in the modulation of disease-resistance responses against these pathogens. Transcriptomics and metabolomics analyses revealed that, in arr6 plants, canonical disease-resistance pathways, like those activated by defensive phytohormones, were not altered, whereas immune responses triggered by microbe-associated molecular patterns were slightly enhanced. Cell-wall composition of arr6 plants was found to be severely altered compared with that of wild-type plants. Remarkably, pectin-enriched cell-wall fractions extracted from arr6 walls triggered more intense immune responses than those activated by similar wall fractions from wild-type plants, suggesting that an-6 pectin fraction is enriched in wall-related damage-associated molecular patterns, which trigger immune responses. This work supports a novel function of ARR6 in the control of cell-wall composition and disease resistance and reinforces the role of the plant cell wall in the modulation of specific immune responses., QC 20200605

The structure of fucoidan isolated from Laminaria hyperborea was elucidatedand chemically tailored in order to obtain a clear structure−function relationship on bioactiveproperties with a minimal amount of variations among the tested molecules. Analysis revealeda sugar composition of 97.8% fucose and 2.2% galactose. Analysis of the glycosidic linkagesshowed (1→3)-α-L-fuco-pyranose (31.9%) to be the dominant residue, followed by 1→2-linked (13.2%) and 1→4-linked (7.7%) fuco-pyranose as well as a high degree of branching(22.4%). Inductively coupled plasma mass spectrometry (ICP-MS) revealed a sulfate contentof 53.8% (degree of sulfation (DS) = 1.7). Raman spectroscopy determined SO4 located axialat 4C and equatorial at 2C as well as an absence of acetylation. SEC-MALS analysisdetermined a high molecular weight (Mw = 469 kDa), suggesting a highly flexible main chainwith short side chains. Both chemical shifts of the fucoidan, proton, and carbon were assignedby NMR and revealed a highly heterogeneous structure in terms of glycosidic linkages.Bioactivity was assessed using a lepirudin-based whole blood model. The immediate responsesby coagulation and complement cascades were measured by prothrombine factor 1 and 2(PTF1.2) and the terminal complement complex (TCC). Cytokines involved in inflammation were detected in a 27-plexcytokine assay. Fucoidan with a high Mw and DS inhibited coagulation, complement, and the cytokines PDGF-BB, RANTES,and IP-10, while activating MCP-1. These effects were obtained at the concentration of 1000 ug/mL and partly at 100 ug/mL.In low concentrations (10 ug/mL), a coagulation stimulating effect of highly sulfated fucoidans (DS = 1.7, Mw = 469 kDa or20.3) was obtained. These data point to a multitude of effects linked to the sulfation degree that needs further mechanisticexploration., QC 20200310

The fungal wall is pivotal for cell shape and function, and in interfacial protection during host infection and environmental challenge. Here, we provide the first description of the carbohydrate composition and structure of the cell wall of the rice blast fungus Magnaporthe oryzae. We focus on the family of glucan elongation proteins (Gels) and characterize five putative beta-1,3-glucan glucanosyltransferases that each carry the Glycoside Hydrolase 72 signature. We generated targeted deletion mutants of all Gel isoforms, that is, the GH72(+), which carry a putative carbohydrate-binding module, and the GH72(-)Gels, without this motif. We reveal that M. oryzae GH72(+) GELs are expressed in spores and during both infective and vegetative growth, but each individual Gel enzymes are dispensable for pathogenicity. Further, we demonstrated that Delta gel1 Delta gel3 Delta gel4 null mutant has a modified cell wall in which 1,3-glucans have a higher degree of polymerization and are less branched than the wild-type strain. The mutant showed significant differences in global patterns of gene expression, a hyper-branching phenotype and no sporulation, and thus was unable to cause rice blast lesions (except via wounded tissues). We conclude that Gel proteins play significant roles in structural modification of the fungal cell wall during appressorium-mediated plant infection., QC 20170510

Arabidopsis heterotrimeric G-protein complex modulates pathogen-associated molecular pattern-triggered immunity (PTI) and disease resistance responses to different types of pathogens. It also plays a role in plant cell wall integrity as mutants impaired in the G- (agb1-2) or G-subunits have an altered wall composition compared with wild-type plants. Here we performed a mutant screen to identify suppressors of agb1-2 (sgb) that restore susceptibility to pathogens to wild-type levels. Out of the four sgb mutants (sgb10-sgb13) identified, sgb11 is a new mutant allele of ESKIMO1 (ESK1), which encodes a plant-specific polysaccharide O-acetyltransferase involved in xylan acetylation. Null alleles (sgb11/esk1-7) of ESK1 restore to wild-type levels the enhanced susceptibility of agb1-2 to the necrotrophic fungus Plectosphaerella cucumerina BMM (PcBMM), but not to the bacterium Pseudomonas syringae pv. tomato DC3000 or to the oomycete Hyaloperonospora arabidopsidis. The enhanced resistance to PcBMM of the agb1-2 esk1-7 double mutant was not the result of the re-activation of deficient PTI responses in agb1-2. Alteration of cell wall xylan acetylation caused by ESK1 impairment was accompanied by an enhanced accumulation of abscisic acid, the constitutive expression of genes encoding antibiotic peptides and enzymes involved in the biosynthesis of tryptophan-derived metabolites, and the accumulation of disease resistance-related secondary metabolites and different osmolites. These esk1-mediated responses counterbalance the defective PTI and PcBMM susceptibility of agb1-2 plants, and explain the enhanced drought resistance of esk1 plants. These results suggest that a deficient PTI-mediated resistance is partially compensated by the activation of specific cell-wall-triggered immune responses. Significance Statement The plant heterotrimeric G protein complex is an essential component of Pathogen Associated Molecular Pattern-triggered immunity (PTI) and of plant disease resistance, QC 20171124

QC 20190211