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6QIX

The crystal structure of Trichuris muris p43

Summary for 6QIX
Entry DOI10.2210/pdb6qix/pdb
DescriptorP43, 2-acetamido-2-deoxy-beta-D-glucopyranose, ACETATE ION, ... (7 entities in total)
Functional Keywordsparasite helminth, unknown function
Biological sourceTrichuris muris (Mouse whipworm)
Total number of polymer chains2
Total formula weight92964.92
Authors
Levy, C.W. (deposition date: 2019-01-21, release date: 2019-06-12, Last modification date: 2024-10-23)
Primary citationBancroft, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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