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  • 6550_Trusch

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DOI

  • F. Trusch
  • L. Loebach
  • S. Wawra
  • E. Durward
  • A. Wuensch
  • Nurul Aqilah Iberahim
  • I. De Bruijn
  • K. MacKenzie
  • A. Willems
  • A. Toloczkoa
  • J. Diéguez-Uribeondo
  • T. Rasmussen
  • T. Schraderf
  • P. Bayer
  • C.J. Secombes
  • P. van West (Corresponding author)
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.
Original languageEnglish
Article number2347
JournalNature Communications
Volume9
DOI
StatePublished - 2018

    Research areas

  • international

ID: 6841819