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

Allison Bancroft, Colin Levy, Thomas Jowitt, Kelly Hayes, Seona Thompson, Edward Mckenzie, Matthew Ball, Eamon Dubaissi, Aidan France, Bruno Bellina, Catherine Sharpe, Aleksandr Mironov, Sheila Brown, Peter Cook, Andrew MacDonald, David Thornton, Richard Grencis

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Article number2344
Pages (from-to)0
JournalNature Communications
Volume10
Issue number1
Early online date28 May 2019
DOIs
Publication statusPublished - 28 May 2019

Research Beacons, Institutes and Platforms

  • Lydia Becker Institute
  • Manchester Institute of Biotechnology

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