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

Sawmynaden, Kovilen
Saouros, Savvas
Marchant, Jan
Simpson, Peter
Bleijlevens, Boris
Blackman, Michael J.
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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 SequenceAnimalsCell Adhesion Molecules/chemistry/metabolismModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein Interaction Domains and MotifsProtozoan Proteins/chemistry/metabolismReceptors, Virus/chemistry/metabolismSequence AlignmentToxoplasma/chemistry
PMID: 18818666
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Research group Biologie d'un parasite intracellulaire obligatoire (773)
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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. doi: 10.1038/embor.2008.179 https://archive-ouverte.unige.ch/unige:2232

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Deposited on : 2009-07-17

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