Host-targeting protein 1 (SpHtp1) from the oomycete Saprolegnia parasitica translocates specifically into fish cells in a tyrosine-O-sulphate-dependent manner.
The eukaryotic oomycetes, 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.
Aberdeen Oomycete Laboratory,University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.
Stephan
S
Wawra
Judith
J
Bain
Elaine
E
Durward
Irene
I
de Bruijn
Kirsty L
KL
Minor
Anja
A
Matena
Lars
L
Löbach
Stephen C
SC
Whisson
Peter
P
Bayer
Andrew J
AJ
Porter
Paul R J
PR
Birch
Chris J
CJ
Secombes
Pieter
P
van West
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D005399:Fishes / Q000382:microbiology*; D011485:Protein Binding; D021382:Protein Sorting Signals; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D044762:Saprolegnia / Q000378:metabolism*; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism
D021382:Protein Sorting Signals; D011506:Proteins; C005662:tyrosine O-sulfate; D014443:Tyrosine