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Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed α-helix

AuthorsPereira, Pedro José Barbosa; Vega, María Cristina ; González-Rey, Elena; Fernández-Carazo, Rafael; Macedo-Ribeiro, Sandra; Gomis-Rüth, F. Xavier ; Gomis-Rüth, F. Xavier ; González, Antonio L.; Coll, Miquel
Keywordsimmunosuppressive agent
protozoal protein
virulence factor
Issue Date2002
PublisherNature Publishing Group
CitationEMBO Reports 3(1): 88-94 (2002)
AbstractThe macrophage infectivity potentiator protein from Trypanosoma cruzi (TcMIP) is a major virulence factor secreted by the etiological agent of Chagas' disease. It is functionally involved in host cell invasion. We have determined the three-dimensional crystal structure of TcMIP at 1.7 Å resolution. The monomeric protein displays a peptidyl-prolyl cis-trans isomerase (PPlase) core, encompassing the characteristic rotamase hydrophobic active site, thus explaining the strong inhibition of TcMIP by the immunosuppressant FK506 and related drugs. In TcMIP, the twisted β-sheet of the core is extended by an extra β-strand, preceded by a long, exposed N-terminal α-helix, which might be a target recognition element. An invasion assay shows that the MIP protein from Legionella pneumophila (LpMIP), which has an equivalent N-terminal α-helix, can substitute for TcMIP. An additional exposed α-helix, this one unique to TcMIP, is located in the C-terminus of the protein. The high-resolution structure reported here opens the possibility for the design of new inhibitory drugs that might be useful for the clinical treatment of American trypanosomiasis.
Publisher version (URL)http://dx.doi.org/10.1093/embo-reports/kvf009
Identifiersdoi: 10.1093/embo-reports/kvf009
issn: 1469-221X
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