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Proteomic Analysis of Phytophthora infestansReveals the Importance of Cell Wall Proteins in Pathogenicity*

Authors :
Resjö, Svante
Brus, Maja
Ali, Ashfaq
Meijer, Harold J.G.
Sandin, Marianne
Govers, Francine
Levander, Fredrik
Grenville-Briggs, Laura
Andreasson, Erik
Source :
Molecular and Cellular Proteomics (MCP Online); November 2017, Vol. 16 Issue: 11 p1958-1971, 14p
Publication Year :
2017

Abstract

The oomycete Phytophthora infestansis the most harmful pathogen of potato. It causes the disease late blight, which generates increased yearly costs of up to one billion euro in the EU alone and is difficult to control. We have performed a large-scale quantitative proteomics study of six P. infestanslife stages with the aim to identify proteins that change in abundance during development, with a focus on preinfectious life stages. Over 10 000 peptides from 2061 proteins were analyzed. We identified several abundance profiles of proteins that were up- or downregulated in different combinations of life stages. One of these profiles contained 59 proteins that were more abundant in germinated cysts and appressoria. A large majority of these proteins were not previously recognized as being appressorial proteins or involved in the infection process. Among those are proteins with putative roles in transport, amino acid metabolism, pathogenicity (including one RXLR effector) and cell wall structure modification. We analyzed the expression of the genes encoding nine of these proteins using RT-qPCR and found an increase in transcript levels during disease progression, in agreement with the hypothesis that these proteins are important in early infection. Among the nine proteins was a group involved in cell wall structure modification and adhesion, including three closely related, uncharacterized proteins encoded by PITG_01131, PITG_01132, and PITG_16135, here denoted Piacwp1–3. Transient silencing of these genes resulted in reduced severity of infection, indicating that these proteins are important for pathogenicity. Our results contribute to further insight into P. infestansbiology, and indicate processes that might be relevant for the pathogen while preparing for host cell penetration and during infection. The mass spectrometry data have been deposited to ProteomeXchange via the PRIDE partner repository with the data set identifier PXD002446.

Details

Language :
English
ISSN :
15359476 and 15359484
Volume :
16
Issue :
11
Database :
Supplemental Index
Journal :
Molecular and Cellular Proteomics (MCP Online)
Publication Type :
Periodical
Accession number :
ejs43709045
Full Text :
https://doi.org/10.1074/mcp.M116.065656