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n6022  (MedChemExpress)
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MedChemExpress n6022
Effects of <t>N6022</t> and SNP on infection structure and host pathogenicity. A) Lesions formed on barley leaves after treatment with 1 m m SNP or N6022. The lesions are observed and the number of lesions is counted after 5 days of inoculation. Asterisks indicate significant differences (*** P < 0.001). B) Lesions formed on rice leaves after treatment with 1 m m SNP or N6022. The lesions are observed and the number of lesions is counted after 5 days of inoculation. Asterisks indicate significant differences (*** P < 0.001). C) Virulence test on wounded rice leaves. Rice leaves were gently scraped with a needle and inoculated with spore solution treated with 1 m m SNP or 1 m m N6022. The length of lesions was measured and recorded after 4 days of inoculation. Asterisks indicate significant differences (** P < 0.01,*** P < 0.001). D) The percentage of septin‐ring formation was calculated for each treatment. Data presented are the mean ± standard errors from three biological replicates ( n = 3), and significant differences compared with the WT are indicated by an asterisk (** P < 0.01, *** P < 0.001). E) Observation on the formation of appressorium septin ring after treatment with 0.5 and 2 m m SNP or N6022. Bar, 5 µm. F) SPR analysis of N6022 binding to GSNOR of M. oryzae and that of rice/human. G) A proposed model of de‐nitrosylation mediated appressorium formation in M. oryzae . During infection of M. oryzae , the appressorium formation accompanied with accumulation of massive NO. H 2 O 2 also contributes to the accumulation of NO. NO and its bioactive donor S‐nitrosoglutathione (GSNO) modify appressorium (AP) proteins through S‐nitrosylation (‐SNO), leading them to inactive proteins. While this process is reversed by the S‐nitrosoglutathione reductase GSNOR‐mediated de‐nitrosylation process, which converts the modification site of ‐SNO into ‐SH form, and oxidized glutathione (GSSG), resulting an increased ratio of GSH/GSSG. The de‐nitrosylated AP proteins are activated for full function, which facilitates appressorium‐related cellular processes and appressorium maturation, leading to a successful infection.
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Effects of N6022 and SNP on infection structure and host pathogenicity. A) Lesions formed on barley leaves after treatment with 1 m m SNP or N6022. The lesions are observed and the number of lesions is counted after 5 days of inoculation. Asterisks indicate significant differences (*** P < 0.001). B) Lesions formed on rice leaves after treatment with 1 m m SNP or N6022. The lesions are observed and the number of lesions is counted after 5 days of inoculation. Asterisks indicate significant differences (*** P < 0.001). C) Virulence test on wounded rice leaves. Rice leaves were gently scraped with a needle and inoculated with spore solution treated with 1 m m SNP or 1 m m N6022. The length of lesions was measured and recorded after 4 days of inoculation. Asterisks indicate significant differences (** P < 0.01,*** P < 0.001). D) The percentage of septin‐ring formation was calculated for each treatment. Data presented are the mean ± standard errors from three biological replicates ( n = 3), and significant differences compared with the WT are indicated by an asterisk (** P < 0.01, *** P < 0.001). E) Observation on the formation of appressorium septin ring after treatment with 0.5 and 2 m m SNP or N6022. Bar, 5 µm. F) SPR analysis of N6022 binding to GSNOR of M. oryzae and that of rice/human. G) A proposed model of de‐nitrosylation mediated appressorium formation in M. oryzae . During infection of M. oryzae , the appressorium formation accompanied with accumulation of massive NO. H 2 O 2 also contributes to the accumulation of NO. NO and its bioactive donor S‐nitrosoglutathione (GSNO) modify appressorium (AP) proteins through S‐nitrosylation (‐SNO), leading them to inactive proteins. While this process is reversed by the S‐nitrosoglutathione reductase GSNOR‐mediated de‐nitrosylation process, which converts the modification site of ‐SNO into ‐SH form, and oxidized glutathione (GSSG), resulting an increased ratio of GSH/GSSG. The de‐nitrosylated AP proteins are activated for full function, which facilitates appressorium‐related cellular processes and appressorium maturation, leading to a successful infection.

Journal: Advanced Science

Article Title: De‐nitrosylation Coordinates Appressorium Function for Infection of the Rice Blast Fungus

doi: 10.1002/advs.202403894

Figure Lengend Snippet: Effects of N6022 and SNP on infection structure and host pathogenicity. A) Lesions formed on barley leaves after treatment with 1 m m SNP or N6022. The lesions are observed and the number of lesions is counted after 5 days of inoculation. Asterisks indicate significant differences (*** P < 0.001). B) Lesions formed on rice leaves after treatment with 1 m m SNP or N6022. The lesions are observed and the number of lesions is counted after 5 days of inoculation. Asterisks indicate significant differences (*** P < 0.001). C) Virulence test on wounded rice leaves. Rice leaves were gently scraped with a needle and inoculated with spore solution treated with 1 m m SNP or 1 m m N6022. The length of lesions was measured and recorded after 4 days of inoculation. Asterisks indicate significant differences (** P < 0.01,*** P < 0.001). D) The percentage of septin‐ring formation was calculated for each treatment. Data presented are the mean ± standard errors from three biological replicates ( n = 3), and significant differences compared with the WT are indicated by an asterisk (** P < 0.01, *** P < 0.001). E) Observation on the formation of appressorium septin ring after treatment with 0.5 and 2 m m SNP or N6022. Bar, 5 µm. F) SPR analysis of N6022 binding to GSNOR of M. oryzae and that of rice/human. G) A proposed model of de‐nitrosylation mediated appressorium formation in M. oryzae . During infection of M. oryzae , the appressorium formation accompanied with accumulation of massive NO. H 2 O 2 also contributes to the accumulation of NO. NO and its bioactive donor S‐nitrosoglutathione (GSNO) modify appressorium (AP) proteins through S‐nitrosylation (‐SNO), leading them to inactive proteins. While this process is reversed by the S‐nitrosoglutathione reductase GSNOR‐mediated de‐nitrosylation process, which converts the modification site of ‐SNO into ‐SH form, and oxidized glutathione (GSSG), resulting an increased ratio of GSH/GSSG. The de‐nitrosylated AP proteins are activated for full function, which facilitates appressorium‐related cellular processes and appressorium maturation, leading to a successful infection.

Article Snippet: To observe the effects of SNP (Biyuntian, Beijing, China), cPTIO (Sigma‐Aldrich, St. Louis, MO, USA), and N6022 (MedChemExpress, USA) treatments, spore suspension (2 × 10 5 spores ml −1 ) of different strains was added with each reagent, then dropped on the hydrophobic coverslip to calculate the appressorium formation rate at 24 hpi.

Techniques: Infection, Binding Assay, Modification