期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 6, 页码 2096-2101出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1113775109
关键词
protein translocation; Phytophthora; Plasmodium
资金
- Biotechnology and Biological Sciences Research Council
- Natural Environment Research Council
- University of Aberdeen
- University of Dundee
- Rural and Environment Research and Analysis Directorate
- Deutsche Forschungsgemeinschaft [TRR 60/1]
- Bundesministerium fur Bildung und Forschung
- Royal Society
- Biotechnology and Biological Sciences Research Council [BB/E007120/1, BB/G012075/1] Funding Source: researchfish
- BBSRC [BB/G012075/1, BB/E007120/1] Funding Source: UKRI
The eukaryoticoomycetes, or water molds, contain several species that are devastating pathogens of plants and animals. During infection, oomycetes translocate effector proteins into host cells, where they interfere with host-defense responses. For several oomycete effectors (i.e., the RxLR-effectors) it has been shown that their N-terminal polypeptides are important for the delivery into the host. Here we demonstrate that the putative RxLR-like effector, host-targeting protein 1 (SpHtp1), from the fish pathogen Saprolegnia parasitica translocates specifically inside host cells. We further demonstrate that cell-surface binding and uptake of this effector protein is mediated by an interaction with tyrosine-O-sulfate-modified cell-surface molecules and not via phospholipids, as has been reported for RxLR-effectors from plant pathogenic oomycetes. These results reveal an effector translocation route based on tyrosine-O-sulfate binding, which could be highly relevant for a wide range of host-microbe interactions.
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