| Autor: |
Trusch, Franziska, Loebach, Lars, Wawra, Stephan, Durward, Elaine, Wuensch, Andreas, Iberahim, Nurul Aqilah, de Bruijin, Irene, MacKenzie, Kevin, Willems, Ariane, Toloczko, Aleksandra, Diéguez-Uribeondo, Javier, Rasmussen, Tim, Schrader, Thomas, Bayer, Peter, Secombes, Chris J., van West, Pieter |
| Předmět: |
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| Zdroj: |
Nature Communications; 6/14/2018, Vol. 9 Issue 1, p1-12, 12p |
| Abstrakt: |
The animal-pathogenic oomycete Saprolegnia parasitica causes serious losses in aquaculture by infecting and killing freshwater fish. Like plant-pathogenic oomycetes, S. parasitica employs similar infection structures and secretes effector proteins that translocate into host cells to manipulate the host. Here, we show that the host-targeting protein SpHtp3 enters fish cells in a pathogen-independent manner. This uptake process is guided by a gp96-like receptor and can be inhibited by supramolecular tweezers. The C-terminus of SpHtp3 (containing the amino acid sequence YKARK), and not the N-terminal RxLR motif, is responsible for the uptake into host cells. Following translocation, SpHtp3 is released from vesicles into the cytoplasm by another host-targeting protein where it degrades nucleic acids. The effector translocation mechanism described here, is potentially also relevant for other pathogen--host interactions as gp96 is found in both animals and plants. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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