| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
|
First published online November 3, 2006; 10.1104/pp.106.090050 Plant Physiology 143:364-377 (2007) © 2007 American Society of Plant Biologists OPEN ACCESS ARTICLE
A Phytophthora infestans Cystatin-Like Protein Targets a Novel Tomato Papain-Like Apoplastic Protease1,[W],[OA]Department of Plant Pathology (M.T., J.W., J.S., S.K.) and Department of Horticulture and Crop Sciences (E.v.d.K.), The Ohio State University, Ohio Agricultural Research and Development Center, Wooster, Ohio 44691; and Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany (R.v.d.H.)
There is emerging evidence that the proteolytic machinery of plants plays important roles in defense against pathogens. The oomycete pathogen Phytophthora infestans, the agent of the devastating late blight disease of tomato (Lycopersicon esculentum) and potato (Solanum tuberosum), has evolved an arsenal of protease inhibitors to overcome the action of host proteases. Previously, we described a family of 14 Kazal-like extracellular serine protease inhibitors from P. infestans. Among these, EPI1 and EPI10 bind and inhibit the pathogenesis-related (PR) P69B subtilisin-like serine protease of tomato. Here, we describe EPIC1 to EPIC4, a new family of P. infestans secreted proteins with similarity to cystatin-like protease inhibitor domains. Among these, the epiC1 and epiC2 genes lacked orthologs in Phytophthora sojae and Phytophthora ramorum, were relatively fast-evolving within P. infestans, and were up-regulated during infection of tomato, suggesting a role during P. infestans-host interactions. Biochemical functional analyses revealed that EPIC2B interacts with and inhibits a novel papain-like extracellular cysteine protease, termed Phytophthora Inhibited Protease 1 (PIP1). Characterization of PIP1 revealed that it is a PR protein closely related to Rcr3, a tomato apoplastic cysteine protease that functions in fungal resistance. Altogether, this and earlier studies suggest that interplay between host proteases of diverse catalytic families and pathogen inhibitors is a general defense-counterdefense process in plant-pathogen interactions.
1 This work was supported by the U.S. Department of Agriculture National Research Initiative (project no. OHO00963–SS) and the National Science Foundation (Plant Genome grant no. DBI–0211659). Salaries and research support also were provided by state and federal funds appropriated to the Ohio Agricultural Research and Development Center, The Ohio State University. 2 These authors contributed equally to the paper. 3 Present address: Department of Plant Pathology, Michigan State University, East Lansing, MI 48824. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Sophien Kamoun (kamoun.1{at}osu.edu). [W] The online version of this article contains Web-only data. [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.106.090050 * Corresponding author; e-mail kamoun.1{at}osu.edu; fax 330–263–3841. Received September 19, 2006; accepted October 24, 2006; published November 3, 2006. This article has been cited by other articles:
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ASPB Publications | PLANT PHYSIOLOGY® | THE PLANT CELL | |
|---|---|---|---|
