Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 39, Pages 16817-16822Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1010575107
Keywords
host-pathogen interactions; innate immunity; malaria; thioester
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Funding
- Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- Welch Foundation [I-1185]
- CNRS
- INSERM
- Fondation pour la Recherche Medicale
- French Ministry of National Education and Research
- European Molecular Biology Organization (EMBO)
- European Commission
- FP7 Cooperation Consortium
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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.
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