Deletion of Aspergillus nidulans cpsA/rseA induces increased extracellular hydrolase production in solid-state culture partly through the high osmolarity glycerol pathway

Ogawa, Mitsuhiro; Wada, Hiroki; Yoshimura, Taro; Sato, Atsushi; Fukuda, Ryouichi; Koyama, Yasuji; Horiuchi, Hiroyuki

doi:10.1016/j.jbiosc.2021.03.002

Cited by 4 publications

(17 citation statements)

References 43 publications

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“…As shown in Figure 3c, the hyphae of ∆FvcpsA were resistant to digestion and produced few protoplasts at 28 • C after 2 h treatment, while the hyphae of the wild type and ∆FvcpsA-C were well digested and generated plentiful protoplasts under the same condition. This is consistent with the results of a recent study showing that ∆CpsA increased tolerance to the lysing enzymes in A. nidulans [22]. These results suggest that FvCpsA plays a critical function in response to environmental stresses in F. verticillioides.…”

Section: Fvcpsa Is Involved In Stress Responsesupporting

confidence: 93%

Glycosyltransferase FvCpsA Regulates Fumonisin Biosynthesis and Virulence in Fusarium verticillioides

et al. 2021

Toxins

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Fusarium verticillioides is the major maize pathogen associated with ear rot and stalk rot worldwide. Fumonisin B1 (FB1) produced by F. verticillioides, poses a serious threat to human and animal health. However, our understanding of FB1 synthesis and virulence mechanism in this fungus is still very limited. Glycosylation catalyzed by glycosyltransferases (GTs) has been identified as contributing to fungal infection and secondary metabolism synthesis. In this study, a family 2 glycosyltransferase, FvCpsA, was identified and characterized in F. verticillioides. ΔFvcpsA exhibited significant defects in vegetative growth. Moreover, ΔFvcpsA also increased resistance to osmotic and cell wall stress agents. In addition, expression levels of FUM genes involved in FB1 production were greatly up-regulated in ΔFvcpsA. HPLC (high performance liquid chromatography) analysis revealed that ΔFvcpsA significantly increased FB1 production. Interestingly, we found that the deletion of FvCPSA showed penetration defects on cellophane membrane, and thus led to obvious defects in pathogenicity. Characterization of FvCpsA domain experiments showed that conserved DXD and QXXRW domains were vital for the biological functions of FvCpsA. Taken together, our results indicate that FvCpsA is critical for fungal growth, FB1 biosynthesis and virulence in F. verticillioides.

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Section: Fvcpsa Is Involved In Stress Responsesupporting

confidence: 93%

Glycosyltransferase FvCpsA Regulates Fumonisin Biosynthesis and Virulence in Fusarium verticillioides

et al. 2021

Toxins

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“…Isolation and characterization of suppressor mutants. Previously, we observed a severe conidiation defect in the rseA deletion mutant 15 . In the present study, we isolated and characterized suppressor mutants, that is, mutant strains in which the conidiation defect of the rseA deletion was suppressed.…”

Section: Resultsmentioning

confidence: 71%

“…We previously reported that extracellular hydrolase production increased in the ΔrseA mutant under a solid-state cultivation condition 15 . To determine whether the srdA deletion contributes to the increased extracellular hydrolase production of the ΔrseA mutant, we examined the extracellular endo-xylanase production by A1145DRDS (Fig.…”

Section: Extracellular Enzyme Production Of the δRseaδsrda Mutantmentioning

confidence: 97%

“…Activation state of intracellular signaling pathways in the ΔrseAΔsrdA mutant. We previously reported that intracellular signaling pathways, such as the HOG and CWI pathways, were highly activated in the rseA deletion mutant 15 . To evaluate the effects of srdA deletion on the activation of these pathways, in the ΔrseA mutant, we determined the phosphorylation states of HogA and MpkA, the mitogen activated protein (MAP) kinases in the HOG and CWI pathways, in A1145DRDS (Fig.…”

Section: Extracellular Enzyme Production Of the δRseaδsrda Mutantmentioning

confidence: 99%

“…Growth sensitivity of the ΔrseAΔsrdA mutant to cell wall perturbating agents. Since the ΔrseA mutant of A. nidulans was highly sensitive to calcofluor white (CFW) and resistant to caspofungin (CAS) 15,26 , we examined the growth sensitivity of A1145DRDS to these cell wall-perturbating agents (Fig. 5C,D).…”

Section: Extracellular Enzyme Production Of the δRseaδsrda Mutantmentioning

confidence: 99%

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srdA mutations suppress the rseA/cpsA deletion mutant conidiation defect in Aspergillus nidulans

Ogawa

Fukuda

Iwama

et al. 2023

Sci Rep

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Conidiation is an important reproductive process in Aspergillus. We previously reported, in A. nidulans, that the deletion of a putative glycosyltransferase gene, rseA/cpsA, causes an increase in the production of extracellular hydrolases and a severe reduction in conidiation. The aim of this study was to obtain novel genetic factors involved in the repression of conidiation in the rseA deletion mutant. We isolated mutants in which the rseA deletion mutant conidiation defect is suppressed and performed a comparative genomic analysis of these mutants. A gene encoding a putative transcription factor was identified as the associated candidate causative gene. The candidate gene was designated as srdA (suppressor gene for the conidiation defect of the rseAdeletion mutant). The conidiation efficiency of the rseAsrdA double-deletion mutant was increased. Introduction of wild-type srdA into the suppressor mutants caused a conidiation defect similar to that of the rseA deletion mutant. Notably, the conidiation efficiencies of the rseAsrdA double-deletion and srdA single-deletion mutants were higher than that of the wild-type strain. These results indicate that srdA is a novel genetic factor that strongly represses conidiation of the rseA deletion mutant, and a putative transcriptional regulator, SrdA is a negative regulator of conidiation in A. nidulans.

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Evidencing New Roles for the Glycosyl-Transferase Cps1 in the Phytopathogenic Fungus Botrytis cinerea

Blandenet

Gonçalves

Rascle

et al. 2022

JoF

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The fungal cell wall occupies a central place in the interaction between fungi and their environment. This study focuses on the role of the putative polysaccharide synthase Cps1 in the physiology, development and virulence of the grey mold-causing agent Botrytis cinerea. Deletion of the Bccps1 gene does not affect the germination of the conidia (asexual spores) or the early mycelial development, but it perturbs hyphal expansion after 24 h, revealing a two-phase hyphal development that has not been reported so far. It causes a severe reduction of mycelial growth in a solid medium and modifies hyphal aggregation into pellets in liquid cultures. It strongly impairs plant penetration, plant colonization and the formation of sclerotia (survival structures). Loss of the BcCps1 protein associates with a decrease in glucans and glycoproteins in the fungus cell wall and the up-accumulation of 132 proteins in the mutant’s exoproteome, among which are fungal cell wall enzymes. This is accompanied by an increased fragility of the mutant mycelium, an increased sensitivity to some environmental stresses and a reduced adhesion to plant surface. Taken together, the results support a significant role of Cps1 in the cell wall biology of B. cinerea.

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Deletion of Aspergillus nidulans cpsA/rseA induces increased extracellular hydrolase production in solid-state culture partly through the high osmolarity glycerol pathway

Cited by 4 publications

References 43 publications

Glycosyltransferase FvCpsA Regulates Fumonisin Biosynthesis and Virulence in Fusarium verticillioides

Glycosyltransferase FvCpsA Regulates Fumonisin Biosynthesis and Virulence in Fusarium verticillioides

srdA mutations suppress the rseA/cpsA deletion mutant conidiation defect in Aspergillus nidulans

Evidencing New Roles for the Glycosyl-Transferase Cps1 in the Phytopathogenic Fungus Botrytis cinerea

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