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A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity
Common in Fungal Extracellular Membrane (CFEM) domain proteins are considered to be unique to fungi and closely related to pathogenicity. However, the Puccinia striiformis f. sp. tritici (Pst) effector containing the CFEM domain has not been reported. Here, we obtained an effector, PstCFEM1, contain...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer Nature Singapore
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10441960/ https://www.ncbi.nlm.nih.gov/pubmed/37676523 http://dx.doi.org/10.1007/s44154-022-00042-5 |
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author | Bai, Xingxuan Peng, Huan Goher, Farhan Islam, Md Ashraful Xu, Sanding Guo, Jia Kang, Zhensheng Guo, Jun |
author_facet | Bai, Xingxuan Peng, Huan Goher, Farhan Islam, Md Ashraful Xu, Sanding Guo, Jia Kang, Zhensheng Guo, Jun |
author_sort | Bai, Xingxuan |
collection | PubMed |
description | Common in Fungal Extracellular Membrane (CFEM) domain proteins are considered to be unique to fungi and closely related to pathogenicity. However, the Puccinia striiformis f. sp. tritici (Pst) effector containing the CFEM domain has not been reported. Here, we obtained an effector, PstCFEM1, containing a functional N-terminal signal peptide sequence and the CFEM domain from Pst race CYR31. qRT-PCR assay indicated that the transcript levels of PstCFEM1 were highly induced during the early stages of infection. Overexpression of PstCFEM1 suppressed Pst322 (an elicitor-like protein of Pst)-trigged cell death, reactive oxygen species (ROS) accumulation and callose deposition. Host-induced gene silencing (HIGS) experiments showed that knockdown of PstCFEM1 decreased the virulence of Pst, while ROS accumulation in silenced plants increased near the infection site. In addition, wheat containing the PstCFEM1-silenced construct increased resistance to multiple races of Pst. Our data suggest that PstCFEM1 suppresses wheat defense by inhibiting ROS accumulation and contributes to increased virulence of Pst. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s44154-022-00042-5. |
format | Online Article Text |
id | pubmed-10441960 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer Nature Singapore |
record_format | MEDLINE/PubMed |
spelling | pubmed-104419602023-08-28 A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity Bai, Xingxuan Peng, Huan Goher, Farhan Islam, Md Ashraful Xu, Sanding Guo, Jia Kang, Zhensheng Guo, Jun Stress Biol Original Paper Common in Fungal Extracellular Membrane (CFEM) domain proteins are considered to be unique to fungi and closely related to pathogenicity. However, the Puccinia striiformis f. sp. tritici (Pst) effector containing the CFEM domain has not been reported. Here, we obtained an effector, PstCFEM1, containing a functional N-terminal signal peptide sequence and the CFEM domain from Pst race CYR31. qRT-PCR assay indicated that the transcript levels of PstCFEM1 were highly induced during the early stages of infection. Overexpression of PstCFEM1 suppressed Pst322 (an elicitor-like protein of Pst)-trigged cell death, reactive oxygen species (ROS) accumulation and callose deposition. Host-induced gene silencing (HIGS) experiments showed that knockdown of PstCFEM1 decreased the virulence of Pst, while ROS accumulation in silenced plants increased near the infection site. In addition, wheat containing the PstCFEM1-silenced construct increased resistance to multiple races of Pst. Our data suggest that PstCFEM1 suppresses wheat defense by inhibiting ROS accumulation and contributes to increased virulence of Pst. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s44154-022-00042-5. Springer Nature Singapore 2022-04-08 /pmc/articles/PMC10441960/ /pubmed/37676523 http://dx.doi.org/10.1007/s44154-022-00042-5 Text en © The Author(s) 2022 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 | Original Paper Bai, Xingxuan Peng, Huan Goher, Farhan Islam, Md Ashraful Xu, Sanding Guo, Jia Kang, Zhensheng Guo, Jun A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
title | A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
title_full | A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
title_fullStr | A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
title_full_unstemmed | A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
title_short | A candidate effector protein PstCFEM1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
title_sort | candidate effector protein pstcfem1 contributes to virulence of stripe rust fungus and impairs wheat immunity |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10441960/ https://www.ncbi.nlm.nih.gov/pubmed/37676523 http://dx.doi.org/10.1007/s44154-022-00042-5 |
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