The sterol-binding activity of PATHOGENESIS-RELATED PROTEIN 1 reveals the mode of action of an antimicrobial protein
- Gamir, Jordi Department of Biology, University of Fribourg, Switzerland
- Darwiche, Rabih Department of Biology, University of Fribourg, Switzerland
- Hof, Pieter van't Department of Biology, University of Fribourg, Switzerland
- Choudhary, Vineet Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
- Stumpe, Michael Department of Biology, University of Fribourg, Switzerland
- Schneiter, Roger Department of Biology, University of Fribourg, Switzerland
- Mauch, Felix Department of Biology, University of Fribourg, Switzerland
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01.02.2017
Published in:
- The Plant Journal. - 2017, vol. 89, no. 3, p. 502–509
English
Pathogenesis-related proteins played a pioneering role 50 years ago in the discovery of plant innate immunity as a set of proteins that accumulated upon pathogen challenge. The most abundant of these proteins, PATHOGENESIS-RELATED 1 (PR-1) encodes a small antimicrobial protein that has become, as a marker of plant immune signaling, one of the most referred to plant proteins. The biochemical activity and mode of action of PR-1 proteins has remained elusive, however. Here, we provide genetic and biochemical evidence for the capacity of PR-1 proteins to bind sterols, and demonstrate that the inhibitory effect on pathogen growth is caused by the sequestration of sterol from pathogens. In support of our findings, sterol-auxotroph pathogens such as the oomycete Phytophthora are particularly sensitive to PR-1, whereas sterol-prototroph fungal pathogens become highly sensitive only when sterol biosynthesis is compromised. Our results are in line with previous findings showing that plants with enhanced PR-1 expression are particularly well protected against oomycete pathogens.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 288538
- DOI 10.1111/tpj.13398
- Persistent URL
- https://folia.unifr.ch/unifr/documents/305452
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