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A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae
Phytopathogens develop specialized infection-related structures to penetrate plant cells during infection. Different from phytopathogens that form appressoria or haustoria, the soil-borne root-infecting fungal pathogen Verticillium dahliae forms hyphopodia during infection, which further differentia...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Nature Singapore
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10423180/ https://www.ncbi.nlm.nih.gov/pubmed/37581020 http://dx.doi.org/10.1007/s42994-023-00102-y |
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author | Ye, Ziqin Qin, Jun Wang, Yu Zhang, Jinghan Wu, Xiaoyun Li, Xiangguo Sun, Lifan Zhang, Jie |
author_facet | Ye, Ziqin Qin, Jun Wang, Yu Zhang, Jinghan Wu, Xiaoyun Li, Xiangguo Sun, Lifan Zhang, Jie |
author_sort | Ye, Ziqin |
collection | PubMed |
description | Phytopathogens develop specialized infection-related structures to penetrate plant cells during infection. Different from phytopathogens that form appressoria or haustoria, the soil-borne root-infecting fungal pathogen Verticillium dahliae forms hyphopodia during infection, which further differentiate into penetration pegs to promote infection. The molecular mechanisms underlying the regulation of hyphopodium formation in V. dahliae remain poorly characterized. Mitogen-activated protein kinases (MAPKs) are highly conserved cytoplasmic kinases that regulate diverse biological processes in eukaryotes. Here we found that deletion of VdKss1, out of the five MAPKs encoded by V. dahliae, significantly impaired V. dahliae hyphopodium formation, in vitro penetration, and pathogenicity in cotton plants. Constitutive activation of MAPK kinase (MAPKK) VdSte7 and MAPK kinase kinase (MAPKKK) VdSte11 specifically activate VdKss1. Deletion of VdSte7 or VdSte11 resulted in a phenotype similar to that of the mutant with VdKss1 deletion. Thus, this study demonstrates that VdSte11-VdSte7-VdKss1 is a core MAPK cascade that regulates hyphopodium formation and pathogenicity in V. dahliae. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s42994-023-00102-y. |
format | Online Article Text |
id | pubmed-10423180 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Springer Nature Singapore |
record_format | MEDLINE/PubMed |
spelling | pubmed-104231802023-08-14 A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae Ye, Ziqin Qin, Jun Wang, Yu Zhang, Jinghan Wu, Xiaoyun Li, Xiangguo Sun, Lifan Zhang, Jie aBIOTECH Research Article Phytopathogens develop specialized infection-related structures to penetrate plant cells during infection. Different from phytopathogens that form appressoria or haustoria, the soil-borne root-infecting fungal pathogen Verticillium dahliae forms hyphopodia during infection, which further differentiate into penetration pegs to promote infection. The molecular mechanisms underlying the regulation of hyphopodium formation in V. dahliae remain poorly characterized. Mitogen-activated protein kinases (MAPKs) are highly conserved cytoplasmic kinases that regulate diverse biological processes in eukaryotes. Here we found that deletion of VdKss1, out of the five MAPKs encoded by V. dahliae, significantly impaired V. dahliae hyphopodium formation, in vitro penetration, and pathogenicity in cotton plants. Constitutive activation of MAPK kinase (MAPKK) VdSte7 and MAPK kinase kinase (MAPKKK) VdSte11 specifically activate VdKss1. Deletion of VdSte7 or VdSte11 resulted in a phenotype similar to that of the mutant with VdKss1 deletion. Thus, this study demonstrates that VdSte11-VdSte7-VdKss1 is a core MAPK cascade that regulates hyphopodium formation and pathogenicity in V. dahliae. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s42994-023-00102-y. Springer Nature Singapore 2023-05-02 /pmc/articles/PMC10423180/ /pubmed/37581020 http://dx.doi.org/10.1007/s42994-023-00102-y Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research Article Ye, Ziqin Qin, Jun Wang, Yu Zhang, Jinghan Wu, Xiaoyun Li, Xiangguo Sun, Lifan Zhang, Jie A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae |
title | A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae |
title_full | A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae |
title_fullStr | A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae |
title_full_unstemmed | A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae |
title_short | A complete MAP kinase cascade controls hyphopodium formation and virulence of Verticillium dahliae |
title_sort | complete map kinase cascade controls hyphopodium formation and virulence of verticillium dahliae |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10423180/ https://www.ncbi.nlm.nih.gov/pubmed/37581020 http://dx.doi.org/10.1007/s42994-023-00102-y |
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