Role of the XylA gene, encoding a cell wall degrading enzyme, during common wheat, durum wheat and barley colonization by Fusarium graminearum

2020 ◽  
Vol 136 ◽  
pp. 103318
Author(s):  
F. Tini ◽  
G. Beccari ◽  
A.H. Benfield ◽  
D.M. Gardiner ◽  
L. Covarelli
Keyword(s):  
Cell Wall ◽  
Durum Wheat ◽  
Fusarium Graminearum ◽  
Common Wheat ◽  
Gene Encoding ◽  
Degrading Enzyme ◽  
Cell Wall Degrading Enzyme ◽  
A Cell ◽  
Xyla Gene

scholarly journals Endopolygalacturonase Is Essential for Citrus Black Rot Caused by Alternaria citri but Not Brown Spot Caused by Alternaria alternata

2001 ◽  
Vol 14 (6) ◽  
pp. 749-757 ◽  
Author(s):  
Atsunori Isshiki ◽  
Kazuya Akimitsu ◽  
Mikihiro Yamamoto ◽  
Hiroyuki Yamamoto
Keyword(s):  
Cell Wall ◽  
Alternaria Alternata ◽  
Biochemical Properties ◽  
Brown Spot ◽  
Black Rot ◽  
Citrus Peel ◽  
Degrading Enzyme ◽  
Cell Wall Degrading Enzyme ◽  
A Cell

Alternaria citri, the cause of Alternaria black rot, and Alternaria alternata rough lemon pathotype, the cause of Alternaria brown spot, are morphologically indistinguishable pathogens of citrus: one causes rot by macerating tissues and the other causes necrotic spots by producing a host-selective toxin. To evaluate the role of endopolygalacturonase (endoPG) in pathogenicity of these two Alternaria spp. pathogens, their genes for endoPG were mutated by gene targeting. The endoPGs produced by these fungi have similar biochemical properties, and the genes are highly similar (99.6% nucleotide identity). The phenotypes of the mutants, however, are completely different. An endoPG mutant of A. citri was significantly reduced in its ability to cause black rot symptoms on citrus as well as in the maceration of potato tissue and could not colonize citrus peel segments. In contrast, an endoPG mutant of A. alternata was unchanged in pathogenicity. The results indicate that a cell wall-degrading enzyme can play different roles in the pathogenicity of fungal pathogens. The role of a cell wall-degrading enzyme depends upon the type of disease but not the taxonomy of the fungus.

scholarly journals Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage  29 tail

2008 ◽  
Vol 105 (28) ◽  
pp. 9552-9557 ◽  
Author(s):  
Y. Xiang ◽  
M. C. Morais ◽  
D. N. Cohen ◽  
V. D. Bowman ◽  
D. L. Anderson ◽  
...  
Keyword(s):  
Cell Wall ◽  
Structural Studies ◽  
Degrading Enzyme ◽  
Cell Wall Degrading Enzyme ◽  
A Cell

Effect of Adding a Cell Wall Degrading Enzyme to a Total Mixed Ration for Lactating Cows1

1996 ◽  
Vol 12 (2) ◽  
pp. 81-85 ◽  
Author(s):  
G.E. Higginbotham ◽  
E.J. Depeters ◽  
S.L. Berry ◽  
A. Ahmadi
Keyword(s):  
Cell Wall ◽  
Total Mixed Ration ◽  
Degrading Enzyme ◽  
Cell Wall Degrading Enzyme ◽  
A Cell

scholarly journals Hyphal fusions in the wood-rotting fungusSchizophyllum commune: I. The effects of incompatibility factors

1970 ◽  
Vol 15 (1) ◽  
pp. 19-28 ◽  
Author(s):  
Sayed S. Ahmad ◽  
Philip G. Miles
Keyword(s):  
Cell Wall ◽  
Mating Type ◽  
Schizophyllum Commune ◽  
Mating Types ◽  
Hyphal Fusion ◽  
Fusion Frequency ◽  
Degrading Enzyme ◽  
Cell Wall Degrading Enzyme ◽  
Incompatibility Factor ◽  
A Cell

SUMMARYEffects of the incompatibility factors inSchizophyllum communeFries on the process of hyphal fusion are described. A role for the A incompatibility factor in hyphal fusion is indicated. Matings between strains with different mating types have higher fusion frequencies than matings between strains with the same mating types. Evidence is presented that the differences in fusion frequencies are not due to genetical factors other than mating types. When two strains of different mating types are grown in the same culture plate, but separated by a cellophane membrane, the strains are altered in some unexplained manner in such a way that even matings between strains of the same mating type have a higher fusion frequency than occurs in matings between compatible strains not so treated. Matings leading to the formation of common-B and dikaryotic mycelia have comparable fusion frequencies while those leading to the formation of common-A mycelia have a far lower frequency of fusions. It has been demonstrated that high fusion frequency is associated with heterozygosity at the A locus. It is suggested that a repression–derepression mechanism involving a cell wall degrading enzyme or enzymes may be involved in the regulation of hyphal fusion.

Role of a Cell-Wall Glucan-degrading Enzyme in Mating of Schizophyllum commune

1967 ◽  
Vol 94 (5) ◽  
pp. 1594-1602 ◽  
Author(s):  
Joseph G. H. Wessels ◽  
Donald J. Niederpruem
Keyword(s):  
Cell Wall ◽  
Schizophyllum Commune ◽  
Degrading Enzyme ◽  
A Cell

scholarly journals Fusarium graminearum FgCWM1 Encodes a Cell Wall Mannoprotein Conferring Sensitivity to Salicylic Acid and Virulence to Wheat

Toxins ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 628 ◽  
Author(s):  
Ya-Zhou Zhang ◽  
Qing Chen ◽  
Cai-Hong Liu ◽  
Lu Lei ◽  
Yang Li ◽  
...  
Keyword(s):  
Cell Wall ◽  
Salicylic Acid ◽  
Fusarium Graminearum ◽  
Defense Responses ◽  
Protein Accumulation ◽  
Head Blight ◽  
Fungal Cell ◽  
Positive Role ◽  
A Cell

Fusarium graminearum causes Fusarium head blight (FHB), a devastating disease of wheat. Salicylic acid (SA) is involved in the resistance of wheat to F. graminearum. Cell wall mannoprotein (CWM) is known to trigger defense responses in plants, but its role in the pathogenicity of F. graminearum remains unclear. Here, we characterized FgCWM1 (FG05_11315), encoding a CWM in F. graminearum. FgCWM1 was highly expressed in wheat spikes by 24 h after initial inoculation and was upregulated by SA. Disruption of FgCWM1 (ΔFgCWM1) reduced mannose and protein accumulation in the fungal cell wall, especially under SA treatment, and resulted in defective fungal cell walls, leading to increased fungal sensitivity to SA. The positive role of FgCWM1 in mannose and protein accumulation was confirmed by its expression in Saccharomyces cerevisiae. Compared with wild type (WT), ΔFgCWM1 exhibited reduced pathogenicity toward wheat, but it produced the same amount of deoxynivalenol both in culture and in spikes. Complementation of ΔFgCWM1 with FgCWM1 restored the WT phenotype. Localization analyses revealed that FgCWM1 was distributed on the cell wall, consistent with its structural role. Thus, FgCWM1 encodes a CWM protein that plays an important role in the cell wall integrity and pathogenicity of F. graminearum.

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