Cargando…
N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease
Hosts and pathogens are engaged in a continuous evolutionary struggle for physiological dominance. A major site of this struggle is the apoplast. In Phytophthora sojae–soybean interactions, PsXEG1, a pathogen-secreted apoplastic endoglucanase, is a key focal point of this struggle, and the subject o...
Autores principales: | , , , , , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7959567/ https://www.ncbi.nlm.nih.gov/pubmed/33082226 http://dx.doi.org/10.1073/pnas.2012149117 |
_version_ | 1783664979739672576 |
---|---|
author | Xia, Yeqiang Ma, Zhenchuan Qiu, Min Guo, Baodian Zhang, Qi Jiang, Haibin Zhang, Baiyu Lin, Yachun Xuan, Mingrun Sun, Liang Shu, Haidong Xiao, Junhua Ye, Wenwu Wang, Yan Wang, Yiming Dong, Suomeng Tyler, Brett M. Wang, Yuanchao |
author_facet | Xia, Yeqiang Ma, Zhenchuan Qiu, Min Guo, Baodian Zhang, Qi Jiang, Haibin Zhang, Baiyu Lin, Yachun Xuan, Mingrun Sun, Liang Shu, Haidong Xiao, Junhua Ye, Wenwu Wang, Yan Wang, Yiming Dong, Suomeng Tyler, Brett M. Wang, Yuanchao |
author_sort | Xia, Yeqiang |
collection | PubMed |
description | Hosts and pathogens are engaged in a continuous evolutionary struggle for physiological dominance. A major site of this struggle is the apoplast. In Phytophthora sojae–soybean interactions, PsXEG1, a pathogen-secreted apoplastic endoglucanase, is a key focal point of this struggle, and the subject of two layers of host defense and pathogen counterdefense. Here, we show that N-glycosylation of PsXEG1 represents an additional layer of this coevolutionary struggle, protecting PsXEG1 against a host apoplastic aspartic protease, GmAP5, that specifically targets PsXEG1. This posttranslational modification also attenuated binding by the previously described host inhibitor, GmGIP1. N-glycosylation of PsXEG1 at N174 and N190 inhibited binding and degradation by GmAP5 and was essential for PsXEG1’s full virulence contribution, except in GmAP5-silenced soybeans. Silencing of GmAP5 reduced soybean resistance against WT P. sojae but not against PsXEG1 deletion strains of P. sojae. The crucial role of N-glycosylation within the three layers of defense and counterdefense centered on PsXEG1 highlight the critical importance of this conserved apoplastic effector and its posttranslational modification in Phytophthora-host coevolutionary conflict. |
format | Online Article Text |
id | pubmed-7959567 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | National Academy of Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-79595672021-03-22 N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease Xia, Yeqiang Ma, Zhenchuan Qiu, Min Guo, Baodian Zhang, Qi Jiang, Haibin Zhang, Baiyu Lin, Yachun Xuan, Mingrun Sun, Liang Shu, Haidong Xiao, Junhua Ye, Wenwu Wang, Yan Wang, Yiming Dong, Suomeng Tyler, Brett M. Wang, Yuanchao Proc Natl Acad Sci U S A Biological Sciences Hosts and pathogens are engaged in a continuous evolutionary struggle for physiological dominance. A major site of this struggle is the apoplast. In Phytophthora sojae–soybean interactions, PsXEG1, a pathogen-secreted apoplastic endoglucanase, is a key focal point of this struggle, and the subject of two layers of host defense and pathogen counterdefense. Here, we show that N-glycosylation of PsXEG1 represents an additional layer of this coevolutionary struggle, protecting PsXEG1 against a host apoplastic aspartic protease, GmAP5, that specifically targets PsXEG1. This posttranslational modification also attenuated binding by the previously described host inhibitor, GmGIP1. N-glycosylation of PsXEG1 at N174 and N190 inhibited binding and degradation by GmAP5 and was essential for PsXEG1’s full virulence contribution, except in GmAP5-silenced soybeans. Silencing of GmAP5 reduced soybean resistance against WT P. sojae but not against PsXEG1 deletion strains of P. sojae. The crucial role of N-glycosylation within the three layers of defense and counterdefense centered on PsXEG1 highlight the critical importance of this conserved apoplastic effector and its posttranslational modification in Phytophthora-host coevolutionary conflict. National Academy of Sciences 2020-11-03 2020-10-20 /pmc/articles/PMC7959567/ /pubmed/33082226 http://dx.doi.org/10.1073/pnas.2012149117 Text en Copyright © 2020 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/ https://creativecommons.org/licenses/by-nc-nd/4.0/This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biological Sciences Xia, Yeqiang Ma, Zhenchuan Qiu, Min Guo, Baodian Zhang, Qi Jiang, Haibin Zhang, Baiyu Lin, Yachun Xuan, Mingrun Sun, Liang Shu, Haidong Xiao, Junhua Ye, Wenwu Wang, Yan Wang, Yiming Dong, Suomeng Tyler, Brett M. Wang, Yuanchao N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease |
title | N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease |
title_full | N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease |
title_fullStr | N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease |
title_full_unstemmed | N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease |
title_short | N-glycosylation shields Phytophthora sojae apoplastic effector PsXEG1 from a specific host aspartic protease |
title_sort | n-glycosylation shields phytophthora sojae apoplastic effector psxeg1 from a specific host aspartic protease |
topic | Biological Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7959567/ https://www.ncbi.nlm.nih.gov/pubmed/33082226 http://dx.doi.org/10.1073/pnas.2012149117 |
work_keys_str_mv | AT xiayeqiang nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT mazhenchuan nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT qiumin nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT guobaodian nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT zhangqi nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT jianghaibin nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT zhangbaiyu nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT linyachun nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT xuanmingrun nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT sunliang nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT shuhaidong nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT xiaojunhua nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT yewenwu nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT wangyan nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT wangyiming nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT dongsuomeng nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT tylerbrettm nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease AT wangyuanchao nglycosylationshieldsphytophthorasojaeapoplasticeffectorpsxeg1fromaspecifichostasparticprotease |