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The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins

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The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins. / Wang, Shumei; Welsh, Lydia; Thorpe, Peter; Whisson, Stephen C; Boevink, Petra C; Birch, Paul R J.

In: mBio, Vol. 9, No. 4, e01216-18, 28.08.2018.

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Wang, S, Welsh, L, Thorpe, P, Whisson, SC, Boevink, PC & Birch, PRJ 2018, 'The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins', mBio, vol. 9, no. 4, e01216-18. https://doi.org/10.1128/mBio.01216-18

APA

Wang, S., Welsh, L., Thorpe, P., Whisson, S. C., Boevink, P. C., & Birch, P. R. J. (2018). The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins. mBio, 9(4), [e01216-18]. https://doi.org/10.1128/mBio.01216-18

Vancouver

Wang S, Welsh L, Thorpe P, Whisson SC, Boevink PC, Birch PRJ. The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins. mBio. 2018 Aug 28;9(4). e01216-18. https://doi.org/10.1128/mBio.01216-18

Author

Wang, Shumei ; Welsh, Lydia ; Thorpe, Peter ; Whisson, Stephen C ; Boevink, Petra C ; Birch, Paul R J. / The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins. In: mBio. 2018 ; Vol. 9, No. 4.

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@article{c0d4926d1fb0438483212bc61088157a,
title = "The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins",
abstract = "The oomycete potato blight pathogen Phytophthora infestans secretes a diverse set of proteins to manipulate host plant immunity. However, there is limited knowledge about how and where they are secreted during infection. Here we used the endoplasmic reticulum (ER)-to-Golgi secretion pathway inhibitor brefeldin A (BFA) in combination with liquid chromatography-electrospray tandem mass spectrometry (LC-MS/MS) to identify extracellular proteins from P. infestans that were conventionally secreted from in vitro-cultured hyphae. We identified 19 proteins with predicted signal peptides that potentially influence plant interactions for which secretion was attenuated by BFA. In addition to inhibition by the apoplastic effector EPIC1, a cysteine protease inhibitor, we show that secretion of the cell wall-degrading pectinesterase enzyme PE1 and the microbe-associated molecular pattern (MAMP)-like elicitin INF4 was inhibited by BFA in vitro and in planta, demonstrating that these proteins are secreted by the conventional, Golgi-mediated pathway. For comparison, secretion of a cytoplasmic RXLR (Arg-[any amino acid]-Leu-Arg) effector, Pi22926, was not inhibited by BFA. During infection, whereas INF4 accumulated outside the plant cell, RXLR effector Pi22926 entered the plant cell and accumulated in the nucleus. The P. infestans effectors, the PE1 enzyme, and INF4 were all secreted from haustoria, pathogen structures that penetrate the plant cell wall to form an intimate interaction with the host plasma membrane. Our findings show the haustorium to be a major site of both conventional and nonconventional secretion of proteins with diverse functions during infection.",
keywords = "Crop disease, Filamentous plant pathogen, Pathogenicity, Secretome, Virulence",
author = "Shumei Wang and Lydia Welsh and Peter Thorpe and Whisson, {Stephen C} and Boevink, {Petra C} and Birch, {Paul R J}",
note = "We are grateful to the China Scholarship Council for funds to support S.W. and to the Biotechnology and Biological Sciences Research Council (BBSRC) (grants BB/N009967/1, BB/L026880/1, and BB/J016500/1) and the Scottish Government Rural and Environment Science and Analytical Services Division (RESAS) for funding provided to P.R.J.B., P.C.B., L.W., and S.C.W.",
year = "2018",
month = "8",
day = "28",
doi = "10.1128/mBio.01216-18",
language = "English",
volume = "9",
journal = "mBio",
issn = "2150-7511",
publisher = "AMER SOC MICROBIOLOGY",
number = "4",

}

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TY - JOUR

T1 - The Phytophthora infestans haustorium is a site for secretion of diverse classes of infection-associated proteins

AU - Wang, Shumei

AU - Welsh, Lydia

AU - Thorpe, Peter

AU - Whisson, Stephen C

AU - Boevink, Petra C

AU - Birch, Paul R J

N1 - We are grateful to the China Scholarship Council for funds to support S.W. and to the Biotechnology and Biological Sciences Research Council (BBSRC) (grants BB/N009967/1, BB/L026880/1, and BB/J016500/1) and the Scottish Government Rural and Environment Science and Analytical Services Division (RESAS) for funding provided to P.R.J.B., P.C.B., L.W., and S.C.W.

PY - 2018/8/28

Y1 - 2018/8/28

N2 - The oomycete potato blight pathogen Phytophthora infestans secretes a diverse set of proteins to manipulate host plant immunity. However, there is limited knowledge about how and where they are secreted during infection. Here we used the endoplasmic reticulum (ER)-to-Golgi secretion pathway inhibitor brefeldin A (BFA) in combination with liquid chromatography-electrospray tandem mass spectrometry (LC-MS/MS) to identify extracellular proteins from P. infestans that were conventionally secreted from in vitro-cultured hyphae. We identified 19 proteins with predicted signal peptides that potentially influence plant interactions for which secretion was attenuated by BFA. In addition to inhibition by the apoplastic effector EPIC1, a cysteine protease inhibitor, we show that secretion of the cell wall-degrading pectinesterase enzyme PE1 and the microbe-associated molecular pattern (MAMP)-like elicitin INF4 was inhibited by BFA in vitro and in planta, demonstrating that these proteins are secreted by the conventional, Golgi-mediated pathway. For comparison, secretion of a cytoplasmic RXLR (Arg-[any amino acid]-Leu-Arg) effector, Pi22926, was not inhibited by BFA. During infection, whereas INF4 accumulated outside the plant cell, RXLR effector Pi22926 entered the plant cell and accumulated in the nucleus. The P. infestans effectors, the PE1 enzyme, and INF4 were all secreted from haustoria, pathogen structures that penetrate the plant cell wall to form an intimate interaction with the host plasma membrane. Our findings show the haustorium to be a major site of both conventional and nonconventional secretion of proteins with diverse functions during infection.

AB - The oomycete potato blight pathogen Phytophthora infestans secretes a diverse set of proteins to manipulate host plant immunity. However, there is limited knowledge about how and where they are secreted during infection. Here we used the endoplasmic reticulum (ER)-to-Golgi secretion pathway inhibitor brefeldin A (BFA) in combination with liquid chromatography-electrospray tandem mass spectrometry (LC-MS/MS) to identify extracellular proteins from P. infestans that were conventionally secreted from in vitro-cultured hyphae. We identified 19 proteins with predicted signal peptides that potentially influence plant interactions for which secretion was attenuated by BFA. In addition to inhibition by the apoplastic effector EPIC1, a cysteine protease inhibitor, we show that secretion of the cell wall-degrading pectinesterase enzyme PE1 and the microbe-associated molecular pattern (MAMP)-like elicitin INF4 was inhibited by BFA in vitro and in planta, demonstrating that these proteins are secreted by the conventional, Golgi-mediated pathway. For comparison, secretion of a cytoplasmic RXLR (Arg-[any amino acid]-Leu-Arg) effector, Pi22926, was not inhibited by BFA. During infection, whereas INF4 accumulated outside the plant cell, RXLR effector Pi22926 entered the plant cell and accumulated in the nucleus. The P. infestans effectors, the PE1 enzyme, and INF4 were all secreted from haustoria, pathogen structures that penetrate the plant cell wall to form an intimate interaction with the host plasma membrane. Our findings show the haustorium to be a major site of both conventional and nonconventional secretion of proteins with diverse functions during infection.

KW - Crop disease

KW - Filamentous plant pathogen

KW - Pathogenicity

KW - Secretome

KW - Virulence

U2 - 10.1128/mBio.01216-18

DO - 10.1128/mBio.01216-18

M3 - Article

VL - 9

JO - mBio

JF - mBio

SN - 2150-7511

IS - 4

M1 - e01216-18

ER -

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