6G9C
Crystal structure of immunomodulatory active chitinase from Trichuris suis, TsES1
Summary for 6G9C
| Entry DOI | 10.2210/pdb6g9c/pdb |
| Descriptor | Immunomodulatory active chitinase, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | tses1, immunomodulatory potential, chitinase, eukaryotic protein expression, lexsy, secretion, dimer, intramolecular disulphide bridge, trichuris suis, hydrolase |
| Biological source | Trichuris suis (pig whipworm) |
| Total number of polymer chains | 2 |
| Total formula weight | 111774.13 |
| Authors | Malecki, P.H.,Balster, K.,Hartmann, S.,Weiss, M.S.,Heinemann, U. (deposition date: 2018-04-10, release date: 2019-04-24, Last modification date: 2024-11-20) |
| Primary citation | Ebner, F.,Lindner, K.,Janek, K.,Niewienda, A.,Malecki, P.H.,Weiss, M.S.,Sutherland, T.E.,Heuser, A.,Kuhl, A.A.,Zentek, J.,Hofmann, A.,Hartmann, S. A Helminth-Derived Chitinase Structurally Similar to Mammalian Chitinase Displays Immunomodulatory Properties in Inflammatory Lung Disease. J Immunol Res, 2021:6234836-6234836, 2021 Cited by PubMed Abstract: Immunomodulation of airway hyperreactivity by excretory-secretory (ES) products of the first larval stage (L1) of the gastrointestinal nematode is reported by us and others. Here, we aimed to identify the proteins accounting for the modulatory effects of the L1 ES proteins and studied six selected L1 proteins for their immunomodulatory efficacy in a murine OVA-induced allergic airway disease model. In particular, an enzymatically active chitinase mediated amelioration of clinical signs of airway hyperreactivity, primarily associated with suppression of eosinophil recruitment into the lung, the associated chemokines, and increased numbers of RELM interstitial lung macrophages. While there is no indication of chitinase directly interfering with dendritic cell activation or antigen presentation to CD4 T cells, treatment of allergic mice with the worm chitinase influenced the hosts' own chitinase activity in the inflamed lung. The three-dimensional structure of the chitinase as determined by high-resolution X-ray crystallography revealed high similarities to mouse acidic mammalian chitinase (AMCase) but a unique ability of chitinase to form dimers. Our data indicate that the structural similarities between the parasite and host chitinase contribute to the disease-ameliorating effect of the helminth-derived chitinase on allergic lung inflammation. PubMed: 34869783DOI: 10.1155/2021/6234836 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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