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A bacterial type III effector targets plant vesicle‐associated membrane proteins
The soilborne bacterial pathogen Ralstonia solanacearum is one of the most destructive plant pathogens worldwide, and its infection process involves the manipulation of numerous plant cellular functions. In this work, we found that the R. solanacearum effector protein RipD partially suppressed diffe...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10423332/ https://www.ncbi.nlm.nih.gov/pubmed/37278116 http://dx.doi.org/10.1111/mpp.13360 |
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author | Wang, Keke Yu, Wenjia Yu, Gang Zhang, Lu Xian, Liu Wei, Yali Perez‐Sancho, Jessica Xue, Hao Rufian, Jose S. Zhuang, Haiyan Kwon, Chian Macho, Alberto P. |
author_facet | Wang, Keke Yu, Wenjia Yu, Gang Zhang, Lu Xian, Liu Wei, Yali Perez‐Sancho, Jessica Xue, Hao Rufian, Jose S. Zhuang, Haiyan Kwon, Chian Macho, Alberto P. |
author_sort | Wang, Keke |
collection | PubMed |
description | The soilborne bacterial pathogen Ralstonia solanacearum is one of the most destructive plant pathogens worldwide, and its infection process involves the manipulation of numerous plant cellular functions. In this work, we found that the R. solanacearum effector protein RipD partially suppressed different levels of plant immunity triggered by R. solanacearum elicitors, including specific responses triggered by pathogen‐associated molecular patterns and secreted effectors. RipD localized in different subcellular compartments in plant cells, including vesicles, and its vesicular localization was enriched in cells undergoing R. solanacearum infection, suggesting that this specific localization may be particularly relevant during infection. Among RipD‐interacting proteins, we identified plant vesicle‐associated membrane proteins (VAMPs). We also found that overexpression of Arabidopsis thaliana VAMP721 and VAMP722 in Nicotiana benthamiana leaves promoted resistance to R. solanacearum, and this was abolished by the simultaneous expression of RipD, suggesting that RipD targets VAMPs to contribute to R. solanacearum virulence. Among proteins secreted in VAMP721/722‐containing vesicles, CCOAOMT1 is an enzyme required for lignin biosynthesis, and mutation of CCOAOMT1 enhanced plant susceptibility to R. solanacearum. Altogether our results reveal the contribution of VAMPs to plant resistance against R. solanacearum and their targeting by a bacterial effector as a pathogen virulence strategy. |
format | Online Article Text |
id | pubmed-10423332 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-104233322023-08-14 A bacterial type III effector targets plant vesicle‐associated membrane proteins Wang, Keke Yu, Wenjia Yu, Gang Zhang, Lu Xian, Liu Wei, Yali Perez‐Sancho, Jessica Xue, Hao Rufian, Jose S. Zhuang, Haiyan Kwon, Chian Macho, Alberto P. Mol Plant Pathol Original Articles The soilborne bacterial pathogen Ralstonia solanacearum is one of the most destructive plant pathogens worldwide, and its infection process involves the manipulation of numerous plant cellular functions. In this work, we found that the R. solanacearum effector protein RipD partially suppressed different levels of plant immunity triggered by R. solanacearum elicitors, including specific responses triggered by pathogen‐associated molecular patterns and secreted effectors. RipD localized in different subcellular compartments in plant cells, including vesicles, and its vesicular localization was enriched in cells undergoing R. solanacearum infection, suggesting that this specific localization may be particularly relevant during infection. Among RipD‐interacting proteins, we identified plant vesicle‐associated membrane proteins (VAMPs). We also found that overexpression of Arabidopsis thaliana VAMP721 and VAMP722 in Nicotiana benthamiana leaves promoted resistance to R. solanacearum, and this was abolished by the simultaneous expression of RipD, suggesting that RipD targets VAMPs to contribute to R. solanacearum virulence. Among proteins secreted in VAMP721/722‐containing vesicles, CCOAOMT1 is an enzyme required for lignin biosynthesis, and mutation of CCOAOMT1 enhanced plant susceptibility to R. solanacearum. Altogether our results reveal the contribution of VAMPs to plant resistance against R. solanacearum and their targeting by a bacterial effector as a pathogen virulence strategy. John Wiley and Sons Inc. 2023-06-05 /pmc/articles/PMC10423332/ /pubmed/37278116 http://dx.doi.org/10.1111/mpp.13360 Text en © 2023 The Authors. Molecular Plant Pathology published by British Society for Plant Pathology and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Original Articles Wang, Keke Yu, Wenjia Yu, Gang Zhang, Lu Xian, Liu Wei, Yali Perez‐Sancho, Jessica Xue, Hao Rufian, Jose S. Zhuang, Haiyan Kwon, Chian Macho, Alberto P. A bacterial type III effector targets plant vesicle‐associated membrane proteins |
title | A bacterial type III effector targets plant vesicle‐associated membrane proteins |
title_full | A bacterial type III effector targets plant vesicle‐associated membrane proteins |
title_fullStr | A bacterial type III effector targets plant vesicle‐associated membrane proteins |
title_full_unstemmed | A bacterial type III effector targets plant vesicle‐associated membrane proteins |
title_short | A bacterial type III effector targets plant vesicle‐associated membrane proteins |
title_sort | bacterial type iii effector targets plant vesicle‐associated membrane proteins |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10423332/ https://www.ncbi.nlm.nih.gov/pubmed/37278116 http://dx.doi.org/10.1111/mpp.13360 |
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