Cleavage of a pathogen apoplastic protein by plant subtilases activates host immunity

© 2020 The Authors New Phytologist © 2020 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 229(2021), 6 vom: 28. März, Seite 3424-3439
1. Verfasser: Wang, Shuaishuai (VerfasserIn)
Weitere Verfasser: Xing, Rongkang, Wang, Yan, Shu, Haidong, Fu, Shenggui, Huang, Jie, Paulus, Judith K, Schuster, Mariana, Saunders, Diane G O, Win, Joe, Vleeshouwers, Vivianne, Wang, Yuanchao, Zheng, Xiaobo, van der Hoorn, Renier A L, Dong, Suomeng
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Phytophthora P69B PC2 apoplast cleavage immunity serine protease small cysteine-rich effector mehr... Plant Proteins Subtilisins EC 3.4.21.- subtilase, plant
Beschreibung
Zusammenfassung:© 2020 The Authors New Phytologist © 2020 New Phytologist Foundation.
The plant apoplast is a harsh environment in which hydrolytic enzymes, especially proteases, accumulate during pathogen infection. However, the defense functions of most apoplastic proteases remain largely elusive. We show here that a newly identified small cysteine-rich secreted protein PC2 from the potato late blight pathogen Phytophthora infestans induces immunity in Solanum plants only after cleavage by plant apoplastic subtilisin-like proteases, such as tomato P69B. A minimal 61 amino acid core peptide carrying two key cysteines, conserved widely in most oomycete species, is sufficient for PC2-induced cell death. Furthermore, we showed that Kazal-like protease inhibitors, such as EPI1, produced by P. infestans prevent PC2 cleavage and dampen PC2 elicited host immunity. This study reveals that cleavage of pathogen proteins to release immunogenic peptides is an important function of plant apoplastic proteases
Beschreibung:Date Completed 14.05.2021
Date Revised 07.12.2022
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.17120