A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex |
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Authors: | Saouros Savvas Edwards-Jones Bryn Reiss Matthias Sawmynaden Kovilen Cota Ernesto Simpson Peter Dowse Timothy J Jäkle Ursula Ramboarina Stephanie Shivarattan Tara Matthews Stephen Soldati-Favre Dominique |
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Affiliation: | Department of Biological Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom. |
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Abstract: | Immediately prior to invasion Toxoplasma gondii tachyzoites release a large number of micronemal proteins (TgMICs) that participate in host cell attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to be identified in T. gondii and has been recently shown to be critical in invasion. This study establishes that the N-terminal thrombospondin type I repeat-like domains (TSR1-like) from TgMIC1 function as an independent adhesin as well as promoting association with TgMIC4. Using the newly solved three-dimensional structure of the C-terminal domain of TgMIC1 we have identified a novel Galectin-like fold that does not possess carbohydrate binding properties and redefines the architecture of TgMIC1. Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism for successful exit from the early secretory compartments and for subsequent trafficking of the complex to the micronemes. |
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