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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...

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Autores principales: 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
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
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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.
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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
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