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PMID: 15096512 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

A Kazal-like extracellular serine protease inhibitor from Phytophthora infestans targets the tomato pathogenesis-related protease P69B.

The Journal of biological chemistry ·Vol. 279 ·No. 25 ·2004-06-18 ·Pages 26370-7

Tian M, Huitema E, Da Cunha L, Torto-Alalibo T, Kamoun S

Abstract

The oomycetes form one of several lineages within the eukaryotes that independently evolved a parasitic lifestyle and consequently are thought to have developed alternative mechanisms of pathogenicity. The oomycete Phytophthora infestans causes late blight, a ravaging disease of potato and tomato. Little is known about processes associated with P. infestans pathogenesis, particularly the suppression of host defense responses. We describe and functionally characterize an extracellular protease inhibitor, EPI1, from P. infestans. EPI1 contains two domains with significant similarity to the Kazal family of serine protease inhibitors. Database searches suggested that Kazal-like proteins are mainly restricted to animals and apicomplexan parasites but appear to be widespread and diverse in the oomycetes. Recombinant EPI1 specifically inhibited subtilisin A among major serine proteases and inhibited and interacted with the pathogenesis-related P69B subtilisin-like serine protease of tomato in intercellular fluids. The epi1 and P69B genes were coordinately expressed and up-regulated during infection of tomato by P. infestans. Inhibition of tomato proteases by EPI1 could form a novel type of defense-counterdefense mechanism between plants and microbial pathogens. In addition, this study points to a common virulence strategy between the oomycete plant pathogen P. infestans and several mammalian parasites, such as the apicomplexan Toxoplasma gondii.

MeSH Terms
Amino Acid Sequence Blotting, Northern Blotting, Western Databases as Topic Electrophoresis, Polyacrylamide Gel Endopeptidases/metabolism Escherichia coli/metabolism Lycopersicon esculentum/microbiology Mass Spectrometry Molecular Sequence Data Phytophthora/enzymology Plant Diseases/microbiology Plasmids/metabolism Precipitin Tests Protein Binding Protein Structure, Tertiary RNA/metabolism Recombinant Proteins/chemistry Reverse Transcriptase Polymerase Chain Reaction Serine Endopeptidases/chemistry Serine Proteinase Inhibitors/chemistry,metabolism,pharmacology Subtilisins/chemistry Time Factors Trypsin Inhibitor, Kazal Pancreatic/chemistry Up-Regulation Virulence
Chemicals
Recombinant Proteins Serine Proteinase Inhibitors Trypsin Inhibitor, Kazal Pancreatic RNA Endopeptidases Serine Endopeptidases Subtilisins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Tian Miaoying
Department of Plant Pathology, The Ohio State University, Ohio Agricultural Research and Development Center, Wooster, Ohio 44691, USA.
Huitema Edgar
Da Cunha Luis
Torto-Alalibo Trudy
Kamoun Sophien
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2004-06-18
Epub
2004-00-19
Pages
26370-7
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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