Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant
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2021
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Trichoderma aggressivum, a mycopathogen causing green mould disease, is a major problem in Agaricus bisporus cultivation due to crop loss, and resistance to chemical fungicides. There is an urgent need for novel biological ways to control mycopathogens without affecting the growth of A. bisporus. Bacteria from the mushroom-casing environment were identified and tested for antagonistic effect on T. aggressivum. Bacillus velezensis produced a large zone of inhibition and its supernatant inhibited the growth of T. aggressivum [−37%], and slightly stimulated A. bisporus growth [+2%]. Label free quantitative-proteomic (LFQ) analysis of changes in the abundance of T. aggressivum proteins following exposure to B. velezensis supernatant indicated increased abundance of proteins associated with catabolic processing of amino acids (40-fold), amino oxidase proteins (14-fold), oxidoreductase proteins (13-fold, 4-fold) and hydrolases (3-fold). Proteins that decreased in relative abundance were anti...oxidants (29-fold), NTF2 domain containing protein (17-fold), 60S ribosomal protein L-13 (14-fold), glucoamylase proteins (13-fold), proteasome subunit proteins (11-fold) and other ribosomal proteins (9-fold). LFQ analysis revealed that exposing A. bisporus to B. velezensis supernatant led to a decrease in: prohibitin (13-fold, 6-fold), proteasomal proteins (11-fold), cytosolic adaptor domain containing protein (5-fold), aldehyde dehydrogenase (4-fold), ribosomal proteins (4-fold), DLH domain-containing protein (4-fold) and PKS_ER domain containing protein (3-fold). The results indicate that A. bisporus was not under stress upon contact with B. velezensis. Whereas a detrimental effect of B. velezensis on T. aggressivum is shown by inhibition of growth and damage-preventing proteins and increased abundance of proteins associated with stress.
Ključne reči:
Agaricus bisporus / Trichoderma aggressivum / Bacillus velezensis / ProteomicsIzvor:
European Journal of Plant Pathology, 2021, 160, 2Izdavač:
- Springer
Finansiranje / projekti:
- Irish Research Council, GOIPD/2018/115
- Q-Exactive mass spectrometer was funded under the SFI Research Infrastructure Call 2012
- Grant Number: 12/RI/2346
Napomena:
- Supplementary information: https://hdl.handle.net/21.15107/rcub_intor_638
Povezane informacije:
- Povezani sadržaj
https://hdl.handle.net/21.15107/rcub_intor_638
Institucija/grupa
TorlakTY - JOUR AU - Kosanović, Dejana AU - Dyas, Maria AU - Grogan, Helen AU - Kavanagh, Kevin PY - 2021 UR - http://intor.torlakinstitut.com/handle/123456789/613 AB - Trichoderma aggressivum, a mycopathogen causing green mould disease, is a major problem in Agaricus bisporus cultivation due to crop loss, and resistance to chemical fungicides. There is an urgent need for novel biological ways to control mycopathogens without affecting the growth of A. bisporus. Bacteria from the mushroom-casing environment were identified and tested for antagonistic effect on T. aggressivum. Bacillus velezensis produced a large zone of inhibition and its supernatant inhibited the growth of T. aggressivum [−37%], and slightly stimulated A. bisporus growth [+2%]. Label free quantitative-proteomic (LFQ) analysis of changes in the abundance of T. aggressivum proteins following exposure to B. velezensis supernatant indicated increased abundance of proteins associated with catabolic processing of amino acids (40-fold), amino oxidase proteins (14-fold), oxidoreductase proteins (13-fold, 4-fold) and hydrolases (3-fold). Proteins that decreased in relative abundance were antioxidants (29-fold), NTF2 domain containing protein (17-fold), 60S ribosomal protein L-13 (14-fold), glucoamylase proteins (13-fold), proteasome subunit proteins (11-fold) and other ribosomal proteins (9-fold). LFQ analysis revealed that exposing A. bisporus to B. velezensis supernatant led to a decrease in: prohibitin (13-fold, 6-fold), proteasomal proteins (11-fold), cytosolic adaptor domain containing protein (5-fold), aldehyde dehydrogenase (4-fold), ribosomal proteins (4-fold), DLH domain-containing protein (4-fold) and PKS_ER domain containing protein (3-fold). The results indicate that A. bisporus was not under stress upon contact with B. velezensis. Whereas a detrimental effect of B. velezensis on T. aggressivum is shown by inhibition of growth and damage-preventing proteins and increased abundance of proteins associated with stress. PB - Springer T2 - European Journal of Plant Pathology T1 - Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant IS - 2 VL - 160 VL - 397 DO - 10.1007/s10658-021-02252-5 ER -
@article{ author = "Kosanović, Dejana and Dyas, Maria and Grogan, Helen and Kavanagh, Kevin", year = "2021", abstract = "Trichoderma aggressivum, a mycopathogen causing green mould disease, is a major problem in Agaricus bisporus cultivation due to crop loss, and resistance to chemical fungicides. There is an urgent need for novel biological ways to control mycopathogens without affecting the growth of A. bisporus. Bacteria from the mushroom-casing environment were identified and tested for antagonistic effect on T. aggressivum. Bacillus velezensis produced a large zone of inhibition and its supernatant inhibited the growth of T. aggressivum [−37%], and slightly stimulated A. bisporus growth [+2%]. Label free quantitative-proteomic (LFQ) analysis of changes in the abundance of T. aggressivum proteins following exposure to B. velezensis supernatant indicated increased abundance of proteins associated with catabolic processing of amino acids (40-fold), amino oxidase proteins (14-fold), oxidoreductase proteins (13-fold, 4-fold) and hydrolases (3-fold). Proteins that decreased in relative abundance were antioxidants (29-fold), NTF2 domain containing protein (17-fold), 60S ribosomal protein L-13 (14-fold), glucoamylase proteins (13-fold), proteasome subunit proteins (11-fold) and other ribosomal proteins (9-fold). LFQ analysis revealed that exposing A. bisporus to B. velezensis supernatant led to a decrease in: prohibitin (13-fold, 6-fold), proteasomal proteins (11-fold), cytosolic adaptor domain containing protein (5-fold), aldehyde dehydrogenase (4-fold), ribosomal proteins (4-fold), DLH domain-containing protein (4-fold) and PKS_ER domain containing protein (3-fold). The results indicate that A. bisporus was not under stress upon contact with B. velezensis. Whereas a detrimental effect of B. velezensis on T. aggressivum is shown by inhibition of growth and damage-preventing proteins and increased abundance of proteins associated with stress.", publisher = "Springer", journal = "European Journal of Plant Pathology", title = "Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant", number = "2", volume = "160, 397", doi = "10.1007/s10658-021-02252-5" }
Kosanović, D., Dyas, M., Grogan, H.,& Kavanagh, K.. (2021). Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant. in European Journal of Plant Pathology Springer., 160(2). https://doi.org/10.1007/s10658-021-02252-5
Kosanović D, Dyas M, Grogan H, Kavanagh K. Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant. in European Journal of Plant Pathology. 2021;160(2). doi:10.1007/s10658-021-02252-5 .
Kosanović, Dejana, Dyas, Maria, Grogan, Helen, Kavanagh, Kevin, "Differential proteomic response of Agaricus bisporus and Trichoderma aggressivum f. europaeum to Bacillus velezensis supernatant" in European Journal of Plant Pathology, 160, no. 2 (2021), https://doi.org/10.1007/s10658-021-02252-5 . .