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Scientific article
English

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

Contributors

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

Published in

EMBO reports, vol. 9, no. 11, p. 1149-1155

Publication date

2008

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

UNIGE affiliation entities

UNIGE research groups

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. 1149–1155. doi: 10.1038/embor.2008.179

Main files (1)

Article (Accepted version)

Identifiers

Additional URL for this publication

http://www.nature.com/embor/journal/v9/n11/full/embor2008179.html

Journal ISSN

1469-221X
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Technical informations

Creation

17/07/2009 11:10:00

First validation

17/07/2009 11:10:00

Update

26/03/2026 10:34:48

Status update

26/03/2026 10:34:48

Last indexation

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