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

Allison J. Bancroft (), Colin W. Levy, Thomas A. Jowitt, Kelly S. Hayes, Seona Thompson, Edward A. Mckenzie, Matthew D. Ball, Eamon Dubaissi, Aidan P. France, Bruno Bellina, Catherine Sharpe, Aleksandr Mironov, Sheila L. Brown, Peter C. Cook, Andrew MacDonald, David J. Thornton and Richard K. Grencis ()
Additional contact information
Allison J. Bancroft: Lydia Becker Institute for Immunology and Inflammation
Colin W. Levy: University of Manchester
Thomas A. Jowitt: Wellcome Trust Centre for Cell Matrix Research
Kelly S. Hayes: Lydia Becker Institute for Immunology and Inflammation
Seona Thompson: Lydia Becker Institute for Immunology and Inflammation
Edward A. Mckenzie: University of Manchester
Matthew D. Ball: University of Manchester
Eamon Dubaissi: Lydia Becker Institute for Immunology and Inflammation
Aidan P. France: University of Manchester
Bruno Bellina: University of Manchester
Catherine Sharpe: Lydia Becker Institute for Immunology and Inflammation
Aleksandr Mironov: University of Manchester
Sheila L. Brown: Lydia Becker Institute for Immunology and Inflammation
Peter C. Cook: Lydia Becker Institute for Immunology and Inflammation
Andrew MacDonald: Lydia Becker Institute for Immunology and Inflammation
David J. Thornton: Lydia Becker Institute for Immunology and Inflammation
Richard K. Grencis: Lydia Becker Institute for Immunology and Inflammation

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-09996-z

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