Host-targeting protein 1 (SpHtp1) from the oomycete Saprolegnia parasitica translocates specifically into fish cells in a tyrosine-O-sulphate-dependent manner. / Wawra, Stephan; Bain, Judith; Durward, Elaine; de Bruijn, Irene; Minor, Kirsty L.; Matena, Anja; Loebach, Lars; Whisson, Stephen C.; Bayer, Peter; Porter, Andrew J.; Birch, Paul R. J.; Secombes, Chris J.; van West, Pieter.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, No. 6, 07.02.2012, p. 2096-2101.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Host-targeting protein 1 (SpHtp1) from the oomycete Saprolegnia parasitica translocates specifically into fish cells in a tyrosine-O-sulphate-dependent manner
A1 - Wawra,Stephan
A1 - Bain,Judith
A1 - Durward,Elaine
A1 - de Bruijn,Irene
A1 - Minor,Kirsty L.
A1 - Matena,Anja
A1 - Loebach,Lars
A1 - Whisson,Stephen C.
A1 - Bayer,Peter
A1 - Porter,Andrew J.
A1 - Birch,Paul R. J.
A1 - Secombes,Chris J.
A1 - van West,Pieter
AU - Wawra,Stephan
AU - Bain,Judith
AU - Durward,Elaine
AU - de Bruijn,Irene
AU - Minor,Kirsty L.
AU - Matena,Anja
AU - Loebach,Lars
AU - Whisson,Stephen C.
AU - Bayer,Peter
AU - Porter,Andrew J.
AU - Birch,Paul R. J.
AU - Secombes,Chris J.
AU - van West,Pieter
PY - 2012/2/7
Y1 - 2012/2/7
N2 - <p>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.</p>
AB - <p>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.</p>
KW - protein translocation
KW - Phytophthora
KW - Plasmodium
KW - PATHOGEN PHYTOPHTHORA-INFESTANS
KW - SOJAE-EFFECTOR AVR1B
KW - PLANT-CELLS
KW - ERYTHROCYTE
KW - SECRETION
KW - VIRULENCE
KW - BINDING
KW - GENOME
KW - ENTRY
KW - AVIRULENCE
U2 - 10.1073/pnas.1113775109
DO - 10.1073/pnas.1113775109
M1 - Article
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 6
VL - 109
SP - 2096
EP - 2101
ER -