A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae
Year: 2010
Type: article
Abstract: The leucine-rich repeat (LRR) proteins LRIM1 and APL1C control the function of the complement-like protein TEP1 in Anopheles mosquitoes. The molecular structure of LRIM1 and APL1C and the basis of their interaction with TEP1 represent a new type of innate immune complex. The LRIM1/APL1C complex specifically binds and solubilizes a cleaved form of TEP1 without an intact thioester bond. The LRIM1 and APL1C LRR domains have a large radius of curvature, glycosylated concave face, and a novel C-terminal capping motif. The LRIM1/APL1C complex is a heterodimer with a single intermolecular disulfide bond. The structure of the LRIM1/APL1C heterodimer reveals an interface between the two LRR domains and an extensive C-terminal coiled-coil domain. We propose that a cleaved form of TEP1 may act as a convertase for activation of other TEP1 molecules and that the LRIM1/APL1C heterodimer regulates formation of this TEP1 convertase.
Institutions: Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Centre National de la Recherche Scientifique, Inserm, Modèles Insectes de l'Immunité Innée, Institut de Biologie Moléculaire et Cellulaire, Culture/s, Patrimoine/s, Création/s - Héritages, Université de Strasbourg
Language: English
Subfield: Immunology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
Funders: Howard Hughes Medical Institute, U.S. Department of Energy, Welch Foundation, European Molecular Biology Organization, University of Chicago, University of Texas Southwestern Medical Center, European Commission, European Synchrotron Radiation Facility, Institut National de la Santé et de la Recherche Médicale, Fondation pour la Recherche Médicale, Centre National de la Recherche Scientifique, Biological and Environmental Research, FP7 Cooperation, Argonne National Laboratory
OpenAlex ID: W2122483092