6QIX

The crystal structure of Trichuris muris p43

6QIX の概要

• エントリーDOI: 10.2210/pdb6qix/pdb
• 分子名称: P43, 2-acetamido-2-deoxy-beta-D-glucopyranose, ACETATE ION, ... (7 entities in total)
• 機能のキーワード: parasite helminth, unknown function
• 由来する生物種: Trichuris muris (Mouse whipworm)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92964.92

構造登録者

Levy, C.W. (登録日: 2019-01-21, 公開日: 2019-06-12, 最終更新日: 2024-10-23)

主引用文献

Bancroft, A.J.,Levy, C.W.,Jowitt, T.A.,Hayes, K.S.,Thompson, S.,Mckenzie, E.A.,Ball, M.D.,Dubaissi, E.,France, A.P.,Bellina, B.,Sharpe, C.,Mironov, A.,Brown, S.L.,Cook, P.C.,S MacDonald, A.,Thornton, D.J.,Grencis, R.K.
The major secreted protein of the whipworm parasite tethers to matrix and inhibits interleukin-13 function.
Nat Commun, 10:2344-2344, 2019

PubMed 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.

PubMed: 31138806
DOI: 10.1038/s41467-019-09996-z

実験手法

X-RAY DIFFRACTION (1.65 Å)