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FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium oxysporum, triggers cell death and modulates plant immunity
Fusarium oxysporum is an important soilborne fungal pathogen with many different formae speciales that can colonize the plant vascular system and cause serious crop wilt disease worldwide. We found a glycoside hydrolase family 12 protein FoEG1, secreted by F. oxysporum, that acted as a pathogen‐asso...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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John Wiley and Sons Inc.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8035634/ https://www.ncbi.nlm.nih.gov/pubmed/33675158 http://dx.doi.org/10.1111/mpp.13041 |
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author | Zhang, Lin Yan, Jianpei Fu, Zhenchao Shi, Wenjiong Ninkuu, Vincent Li, Guangyue Yang, Xiufen Zeng, Hongmei |
author_facet | Zhang, Lin Yan, Jianpei Fu, Zhenchao Shi, Wenjiong Ninkuu, Vincent Li, Guangyue Yang, Xiufen Zeng, Hongmei |
author_sort | Zhang, Lin |
collection | PubMed |
description | Fusarium oxysporum is an important soilborne fungal pathogen with many different formae speciales that can colonize the plant vascular system and cause serious crop wilt disease worldwide. We found a glycoside hydrolase family 12 protein FoEG1, secreted by F. oxysporum, that acted as a pathogen‐associated molecular pattern (PAMP) targeting the apoplast of plants to induce cell death. Purified FoEG1 protein triggered cell death in different plants and induced the plant defence response to enhance the disease resistance of plants. The ability of FoEG1 to induce cell death was mediated by leucine‐rich repeat (LRR) receptor‐like kinases BAK1 and SOBIR1, and this ability was independent of its hydrolase activity. The mutants of cysteine residues did not affect the ability of FoEG1 to induce cell death, and an 86 amino acid fragment from amino acid positions 144 to 229 of FoEG1 was sufficient to induce cell death in Nicotiana benthamiana. In addition, the expression of FoEG1 was strongly induced in the early stage of F. oxysporum infection of host plants, and FoEG1 deletion or loss of enzyme activity reduced the virulence of F. oxysporum. Therefore, our results suggest that FoEG1 can contribute to the virulence of F. oxysporum depending on its enzyme activity and can also act as a PAMP to induce plant defence responses. |
format | Online Article Text |
id | pubmed-8035634 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-80356342021-04-15 FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium oxysporum, triggers cell death and modulates plant immunity Zhang, Lin Yan, Jianpei Fu, Zhenchao Shi, Wenjiong Ninkuu, Vincent Li, Guangyue Yang, Xiufen Zeng, Hongmei Mol Plant Pathol Original Articles Fusarium oxysporum is an important soilborne fungal pathogen with many different formae speciales that can colonize the plant vascular system and cause serious crop wilt disease worldwide. We found a glycoside hydrolase family 12 protein FoEG1, secreted by F. oxysporum, that acted as a pathogen‐associated molecular pattern (PAMP) targeting the apoplast of plants to induce cell death. Purified FoEG1 protein triggered cell death in different plants and induced the plant defence response to enhance the disease resistance of plants. The ability of FoEG1 to induce cell death was mediated by leucine‐rich repeat (LRR) receptor‐like kinases BAK1 and SOBIR1, and this ability was independent of its hydrolase activity. The mutants of cysteine residues did not affect the ability of FoEG1 to induce cell death, and an 86 amino acid fragment from amino acid positions 144 to 229 of FoEG1 was sufficient to induce cell death in Nicotiana benthamiana. In addition, the expression of FoEG1 was strongly induced in the early stage of F. oxysporum infection of host plants, and FoEG1 deletion or loss of enzyme activity reduced the virulence of F. oxysporum. Therefore, our results suggest that FoEG1 can contribute to the virulence of F. oxysporum depending on its enzyme activity and can also act as a PAMP to induce plant defence responses. John Wiley and Sons Inc. 2021-03-05 /pmc/articles/PMC8035634/ /pubmed/33675158 http://dx.doi.org/10.1111/mpp.13041 Text en © 2021 The Authors. Molecular Plant Pathology published by British Society for Plant Pathology and John Wiley & Sons Ltd https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Original Articles Zhang, Lin Yan, Jianpei Fu, Zhenchao Shi, Wenjiong Ninkuu, Vincent Li, Guangyue Yang, Xiufen Zeng, Hongmei FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium oxysporum, triggers cell death and modulates plant immunity |
title | FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium
oxysporum, triggers cell death and modulates plant immunity |
title_full | FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium
oxysporum, triggers cell death and modulates plant immunity |
title_fullStr | FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium
oxysporum, triggers cell death and modulates plant immunity |
title_full_unstemmed | FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium
oxysporum, triggers cell death and modulates plant immunity |
title_short | FoEG1, a secreted glycoside hydrolase family 12 protein from Fusarium
oxysporum, triggers cell death and modulates plant immunity |
title_sort | foeg1, a secreted glycoside hydrolase family 12 protein from fusarium
oxysporum, triggers cell death and modulates plant immunity |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8035634/ https://www.ncbi.nlm.nih.gov/pubmed/33675158 http://dx.doi.org/10.1111/mpp.13041 |
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