PMID:16166092

Citation	Saouros, S, Edwards-Jones, B, Reiss, M, Sawmynaden, K, Cota, E, Simpson, P, Dowse, TJ, Jäkle, U, Ramboarina, S, Shivarattan, T, Matthews, S and Soldati-Favre, D (2005) A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. J. Biol. Chem. 280:38583-91
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.
Links	PubMed Online version:10.1074/jbc.C500365200
Keywords	Animals; Blotting, Western; Carbohydrates/chemistry; Cell Adhesion; Cell Adhesion Molecules/chemistry; Cell Adhesion Molecules/metabolism; Cell Adhesion Molecules/physiology; Cloning, Molecular; Endoplasmic Reticulum/metabolism; Escherichia coli/metabolism; Fluorescent Antibody Technique, Indirect; Galectins/chemistry; Golgi Apparatus/metabolism; Humans; Immunoprecipitation; Magnetic Resonance Spectroscopy; Microscopy, Confocal; Microscopy, Fluorescence; Models, Biological; Molecular Conformation; Neoplasm Invasiveness; Pichia/metabolism; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Protozoan Proteins/chemistry; Protozoan Proteins/metabolism; Protozoan Proteins/physiology; Thrombospondins/metabolism; Toxoplasma/metabolism; Transfection
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