2017
DOI: 10.1016/j.pmpp.2016.10.002
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Differences in the expression profile of endo-β-(1,6)- d -galactanase in pathogenic and non-pathogenic races of Colletotrichum lindemuthianum grown in the presence of arabinogalactan, xylan or Phaseolus vulgaris cell walls

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Cited by 2 publications
(8 citation statements)
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“…There are no crystallized structures of endo1,6GAL and 1,6GAL; however, a prediction of the three-dimensional structure of Colletotrichum lindemuthianum endo1,6GAL has been reported. The endo1,6GAL model adopts a (β/α)8 TIM barrel fold topology (eight-stranded parallel β-strand, forming a central barrel surrounded by eight α-helices) with a putative active site located at the C-terminus, which is consistent with the characteristic structure of GH30 family enzymes ( Figure 2C ; Villa-Rivera et al, 2017b ). These enzymes have been characterized from fungi and bacteria and have also been expressed in heterologous models ( Table 1 ).…”
Section: Degradation Of Ags By Enzymes Of Microorganismssupporting
confidence: 68%
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“…There are no crystallized structures of endo1,6GAL and 1,6GAL; however, a prediction of the three-dimensional structure of Colletotrichum lindemuthianum endo1,6GAL has been reported. The endo1,6GAL model adopts a (β/α)8 TIM barrel fold topology (eight-stranded parallel β-strand, forming a central barrel surrounded by eight α-helices) with a putative active site located at the C-terminus, which is consistent with the characteristic structure of GH30 family enzymes ( Figure 2C ; Villa-Rivera et al, 2017b ). These enzymes have been characterized from fungi and bacteria and have also been expressed in heterologous models ( Table 1 ).…”
Section: Degradation Of Ags By Enzymes Of Microorganismssupporting
confidence: 68%
“…Deletion of the MoAbfB gene encoding an α -N- arabinofuranosidase B from Magnaporthe oryzae resulted in a reduction in disease severity in rice ( Wu et al, 2016 ). Likewise, comparison of the genetic expression of an endo1,6GAL between pathogenic and non-pathogenic strains of C. lindemuthianum , showed that compared with most of the evaluated conditions, the levels of genetic expression were higher in pathogenic than non-pathogenic strains, supporting a role for this enzyme in the PCW degradation during the establishment of the infection ( Villa-Rivera et al, 2017b ). Finally, the inactivation of Malus domestica AGPs with β-Glc Yariv reagent, which exhibit an effect similar to that of degradation by enzymes, causes a more rapid progress of Penicillium spinulosum infection, thus reinforcing the notion that the inactivation of AG type II has an impact on the PCW integrity and the activation of plant defense responses ( Leszczuk et al, 2019 ).…”
Section: Ags Hydrolysis and Plant-microbe Interactionsmentioning
confidence: 95%
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“…Xylan is the second most abundant polysaccharide in PCW and consists of a backbone of β-(1,4)-D-xylose that can be branched by different glycosidic residues, such as L-arabinofuranose, L-arabinopiranose, L-rhamnose, D-glucuronic acid, and D-galacturonic acid, which can bind to the ends of the pectic polysaccharides and cellulose fibers [ 34 , 35 ]. In cultures with glucose as the carbon source, P0 and P1472 showed low levels of XYL activity ( Figure 2 A), in agreement with previous reports [ 14 , 26 ] and consistent with the CCR of hydrolytic enzyme-encoding genes in filamentous fungi [ 36 , 37 , 38 ].…”
Section: Resultssupporting
confidence: 92%
“…Previously, we found that two pathotypes of C. lindemuthianum (pathogenic P1472 and non-pathogenic P0) showed differential gene expression and/or secretion levels of pectin lyase, endo-1,4-β-D-xylanase, and β-galactosidase in cultures with pectin, polygalacturonic acid, arabinogalactan, xylan, and PCW from P. vulgaris as carbon sources, suggesting a relationship with their lifestyle differences [ 11 , 12 , 14 , 26 ]. Furthermore, these findings suggest the differential production of PCWDEs with biotechnological potential.…”
Section: Introductionmentioning
confidence: 99%