The major secreted protein of the whipworm parasite tethers to matrix and inhibits interleukin-13 functionCitation formats

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The major secreted protein of the whipworm parasite tethers to matrix and inhibits interleukin-13 function. / Bancroft, Allison; Levy, Colin; Jowitt, Thomas; Hayes, Kelly; Thompson, Seona; Mckenzie, Edward; Ball, Matthew; Dubaissi, Eamon; France, Aidan; Bellina, Bruno; Sharpe, Catherine; Mironov, Aleksandr; Brown, Sheila; Cook, Peter; MacDonald, Andrew; Thornton, David; Grencis, Richard.

In: Nature Communications, Vol. 10, No. 1, 2344, 28.05.2019, p. 0.

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Bancroft, Allison ; Levy, Colin ; Jowitt, Thomas ; Hayes, Kelly ; Thompson, Seona ; Mckenzie, Edward ; Ball, Matthew ; Dubaissi, Eamon ; France, Aidan ; Bellina, Bruno ; Sharpe, Catherine ; Mironov, Aleksandr ; Brown, Sheila ; Cook, Peter ; MacDonald, Andrew ; Thornton, David ; Grencis, Richard. / The major secreted protein of the whipworm parasite tethers to matrix and inhibits interleukin-13 function. In: Nature Communications. 2019 ; Vol. 10, No. 1. pp. 0.

Bibtex

@article{8d4dcce0b37342c2962b82d68c632313,
title = "The major secreted protein of the whipworm parasite tethers to matrix and inhibits interleukin-13 function",
abstract = "Infection by soil transmitted parasitic helminths, such as Trichuris spp, are ubiquitous in humans and animals but the mechanisms determining persistence of chronic infections are poorly understood. Here we show that p43, the single most abundant protein in T. muris excretions/secretions, is non-immunogenic during infection and has an unusual sequence and structure containing subdomain homology to thrombospondin type 1 and interleukin (IL)−13 receptor (R) α2. Binding of p43 to IL-13, the key effector cytokine responsible for T. muris expulsion, inhibits IL-13 function both in vitro and in vivo. Tethering of p43 to matrix proteoglycans presents a bound source of p43 to facilitate interaction with IL-13, which may underpin chronic intestinal infection. Our results suggest that exploiting the biology of p43 may open up new approaches to modulating IL-13 function and control of Trichuris infections.",
author = "Allison Bancroft and Colin Levy and Thomas Jowitt and Kelly Hayes and Seona Thompson and Edward Mckenzie and Matthew Ball and Eamon Dubaissi and Aidan France and Bruno Bellina and Catherine Sharpe and Aleksandr Mironov and Sheila Brown and Peter Cook and Andrew MacDonald and David Thornton and Richard Grencis",
year = "2019",
month = may,
day = "28",
doi = "10.1038/s41467-019-09996-z",
language = "English",
volume = "10",
pages = "0",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Springer Nature",
number = "1",

}

RIS

TY - JOUR

T1 - The major secreted protein of the whipworm parasite tethers to matrix and inhibits interleukin-13 function

AU - Bancroft, Allison

AU - Levy, Colin

AU - Jowitt, Thomas

AU - Hayes, Kelly

AU - Thompson, Seona

AU - Mckenzie, Edward

AU - Ball, Matthew

AU - Dubaissi, Eamon

AU - France, Aidan

AU - Bellina, Bruno

AU - Sharpe, Catherine

AU - Mironov, Aleksandr

AU - Brown, Sheila

AU - Cook, Peter

AU - MacDonald, Andrew

AU - Thornton, David

AU - Grencis, Richard

PY - 2019/5/28

Y1 - 2019/5/28

N2 - Infection by soil transmitted parasitic helminths, such as Trichuris spp, are ubiquitous in humans and animals but the mechanisms determining persistence of chronic infections are poorly understood. Here we show that p43, the single most abundant protein in T. muris excretions/secretions, is non-immunogenic during infection and has an unusual sequence and structure containing subdomain homology to thrombospondin type 1 and interleukin (IL)−13 receptor (R) α2. Binding of p43 to IL-13, the key effector cytokine responsible for T. muris expulsion, inhibits IL-13 function both in vitro and in vivo. Tethering of p43 to matrix proteoglycans presents a bound source of p43 to facilitate interaction with IL-13, which may underpin chronic intestinal infection. Our results suggest that exploiting the biology of p43 may open up new approaches to modulating IL-13 function and control of Trichuris infections.

AB - Infection by soil transmitted parasitic helminths, such as Trichuris spp, are ubiquitous in humans and animals but the mechanisms determining persistence of chronic infections are poorly understood. Here we show that p43, the single most abundant protein in T. muris excretions/secretions, is non-immunogenic during infection and has an unusual sequence and structure containing subdomain homology to thrombospondin type 1 and interleukin (IL)−13 receptor (R) α2. Binding of p43 to IL-13, the key effector cytokine responsible for T. muris expulsion, inhibits IL-13 function both in vitro and in vivo. Tethering of p43 to matrix proteoglycans presents a bound source of p43 to facilitate interaction with IL-13, which may underpin chronic intestinal infection. Our results suggest that exploiting the biology of p43 may open up new approaches to modulating IL-13 function and control of Trichuris infections.

U2 - 10.1038/s41467-019-09996-z

DO - 10.1038/s41467-019-09996-z

M3 - Article

C2 - 31138806

VL - 10

SP - 0

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 2344

ER -