A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex

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

doi:10.1074/jbc.C500365200

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Title		A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex
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 show all authors [1 - 12]
Published in		The Journal of biological chemistry. 2005, vol. 280, no. 46, p. 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.
Keywords		Animals — Blotting, Western — Carbohydrates/chemistry — Cell Adhesion — Cell Adhesion Molecules/chemistry/metabolism/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/metabolism/physiology — Thrombospondins/metabolism — Toxoplasma/metabolism — Transfection
Identifiers		DOI: 10.1074/jbc.C500365200 PMID: 16166092
Full text		Article (Accepted version) (677 Kb) - Free access Other version: http://www.jbc.org/content/280/46/38583.long
Structures		Faculté de médecine / Section de médecine fondamentale / Département de microbiologie et médecine moléculaire
Research group		Biologie d'un parasite intracellulaire obligatoire (773)
Citation (ISO format)		SAOUROS, Savvas et al. A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. In: The Journal of biological chemistry, 2005, vol. 280, n° 46, p. 38583-91. doi: 10.1074/jbc.C500365200 https://archive-ouverte.unige.ch/unige:3971