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The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei
Anthracnose, caused by the ascomycete fungus Colletotrichum scovillei, is a destructive disease in pepper. The fungus germinates and develops an infection structure called an appressorium on the plant surface. Several signaling cascades, including cAMP-mediated signaling and mitogen-activated protei...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Korean Society of Plant Pathology
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9742795/ https://www.ncbi.nlm.nih.gov/pubmed/36503188 http://dx.doi.org/10.5423/PPJ.OA.06.2022.0074 |
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author | Shin, Jong-Hwan Park, Byung-Seong Kim, Kyoung Su |
author_facet | Shin, Jong-Hwan Park, Byung-Seong Kim, Kyoung Su |
author_sort | Shin, Jong-Hwan |
collection | PubMed |
description | Anthracnose, caused by the ascomycete fungus Colletotrichum scovillei, is a destructive disease in pepper. The fungus germinates and develops an infection structure called an appressorium on the plant surface. Several signaling cascades, including cAMP-mediated signaling and mitogen-activated protein kinase (MAPK) cascades, are involved in fungal development and pathogenicity in plant pathogenic fungi, but this has not been well studied in the fruit-infecting fungus C. scovillei. Ste50 is an adaptor protein interacting with multiple upstream components to activate the MAPK cascades. Here, we characterized the CsSTE50 gene of C. scovillei, a homolog of Magnaporthe oryzae MST50 that functions in MAPK cascades, by gene knockout. The knockout mutant ΔCsste50 had pleiotropic phenotypes in development and pathogenicity. Compared with the wild-type, the mutants grew faster and produced more conidia on regular agar but were more sensitive to osmotic stress. On artificial and plant surfaces, the conidia of the mutant showed significantly reduced germination and failed to form appressoria. The mutant was completely non-pathogenic on pepper fruits with or without wounds, indicating that pre-penetration and invasive growth were both defective in the mutant. Our results show that the adaptor protein CsSTE50 plays a role in vegetative growth, conidiation, germination, appressorium formation, and pathogenicity in C. scovillei. |
format | Online Article Text |
id | pubmed-9742795 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Korean Society of Plant Pathology |
record_format | MEDLINE/PubMed |
spelling | pubmed-97427952022-12-20 The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei Shin, Jong-Hwan Park, Byung-Seong Kim, Kyoung Su Plant Pathol J Research Article Anthracnose, caused by the ascomycete fungus Colletotrichum scovillei, is a destructive disease in pepper. The fungus germinates and develops an infection structure called an appressorium on the plant surface. Several signaling cascades, including cAMP-mediated signaling and mitogen-activated protein kinase (MAPK) cascades, are involved in fungal development and pathogenicity in plant pathogenic fungi, but this has not been well studied in the fruit-infecting fungus C. scovillei. Ste50 is an adaptor protein interacting with multiple upstream components to activate the MAPK cascades. Here, we characterized the CsSTE50 gene of C. scovillei, a homolog of Magnaporthe oryzae MST50 that functions in MAPK cascades, by gene knockout. The knockout mutant ΔCsste50 had pleiotropic phenotypes in development and pathogenicity. Compared with the wild-type, the mutants grew faster and produced more conidia on regular agar but were more sensitive to osmotic stress. On artificial and plant surfaces, the conidia of the mutant showed significantly reduced germination and failed to form appressoria. The mutant was completely non-pathogenic on pepper fruits with or without wounds, indicating that pre-penetration and invasive growth were both defective in the mutant. Our results show that the adaptor protein CsSTE50 plays a role in vegetative growth, conidiation, germination, appressorium formation, and pathogenicity in C. scovillei. Korean Society of Plant Pathology 2022-12 2022-12-01 /pmc/articles/PMC9742795/ /pubmed/36503188 http://dx.doi.org/10.5423/PPJ.OA.06.2022.0074 Text en © The Korean Society of Plant Pathology https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0 (https://creativecommons.org/licenses/by-nc/4.0/) ) which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Shin, Jong-Hwan Park, Byung-Seong Kim, Kyoung Su The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei |
title | The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei |
title_full | The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei |
title_fullStr | The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei |
title_full_unstemmed | The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei |
title_short | The CsSTE50 Adaptor Protein in Mitogen-Activated Protein Kinase Cascades Is Essential for Pepper Anthracnose Disease of Colletotrichum scovillei |
title_sort | csste50 adaptor protein in mitogen-activated protein kinase cascades is essential for pepper anthracnose disease of colletotrichum scovillei |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9742795/ https://www.ncbi.nlm.nih.gov/pubmed/36503188 http://dx.doi.org/10.5423/PPJ.OA.06.2022.0074 |
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