Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition

Sawmynaden, Kovilen; Saouros, Savvas; Friedrich, Nikolas; Marchant, Jan; Simpson, Peter; Bleijlevens, Boris; Blackman, Michael J.; Soldati-Favre, Dominique; Matthews, Stephen

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Title		Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition
Authors		Sawmynaden, Kovilen Saouros, Savvas Friedrich, Nikolas Marchant, Jan Simpson, Peter Bleijlevens, Boris Blackman, Michael J. Soldati-Favre, Dominique Matthews, Stephen show all authors [1 - 9]
Published in		EMBO Reports. 2008, vol. 9, no. 11, p. 1149-55
Abstract		The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Adhesive complexes composed of microneme proteins (MICs) are secreted onto the parasite surface from intracellular stores and fulfil crucial roles in host-cell recognition, attachment and penetration. Here, we report the high-resolution solution structure of a complex between two crucial MICs, TgMIC6 and TgMIC1. Furthermore, we identify two analogous interaction sites within separate epidermal growth factor-like (EGF) domains of TgMIC6-EGF2 and EGF3-and confirm that both interactions are functional for the recognition of host cell receptor in the parasite, using immunofluorescence and invasion assays. The nature of this new mode of recognition of the EGF domain and its abundance in apicomplexan surface proteins suggest a more generalized means of constructing functional assemblies by using EGF domains with highly specific receptor-binding properties.
Keywords		Amino Acid Sequence — Animals — Cell Adhesion Molecules/chemistry/metabolism — Models, Molecular — Molecular Sequence Data — Nuclear Magnetic Resonance, Biomolecular — Protein Interaction Domains and Motifs — Protozoan Proteins/chemistry/metabolism — Receptors, Virus/chemistry/metabolism — Sequence Alignment — Toxoplasma/chemistry
Identifiers		DOI: 10.1038/embor.2008.179 PMID: 18818666
Full text		Article (Author postprint) (1.8 MB) - Limited access to UNIGE Other version: http://www.nature.com/embor/journal/v9/n11/full/embor2008179.html
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)		SAWMYNADEN, Kovilen et al. Structural insights into microneme protein assembly reveal a new mode of EGF domain recognition. In: EMBO reports, 2008, vol. 9, n° 11, p. 1149-55. https://archive-ouverte.unige.ch/unige:2232