Baxter Richard H, Steinert Stefanie, Chelliah Y, Volohonsky Gloria, Levashina Elena A, Deisenhofer J
A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae Article de journal
Dans: vol. 107, no. 39, p. 16817-22, 2010.
Résumé | Liens | BibTeX | Étiquettes: APL1C, LRIM1
@article{RH2010,
title = {A heterodimeric complex of the LRR proteins LRIM1 and APL1C regulates complement-like immunity in Anopheles gambiae},
author = {Richard H Baxter and Stefanie Steinert and Y Chelliah and Gloria Volohonsky and Elena A Levashina and J Deisenhofer},
url = {http://www.ncbi.nlm.nih.gov/pubmed/20826443},
year = {2010},
date = {2010-09-08},
volume = {107},
number = {39},
pages = {16817-22},
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.},
keywords = {APL1C, LRIM1},
pubstate = {published},
tppubtype = {article}
}
Fraiture Malou, Baxter Richard H G, Steinert Stefanie, Chelliah Yogarany, Frolet Cécile, Quispe-Tintaya Wilber, Hoffmann Jules A, Blandin Stéphanie A, Levashina Elena A
Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium Article de journal
Dans: Cell Host Microbe, vol. 5, no. 3, p. 273–284, 2009, ISSN: 1934-6069.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anopheles, APL1, Biological, blandin, Complement System Proteins, Hemolymph, hoffmann, Immunologic Factors, LRIM1, M3i, Models, Plasmodium, Protein Binding, Proteins, TEP1
@article{fraiture_two_2009,
title = {Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium},
author = {Malou Fraiture and Richard H G Baxter and Stefanie Steinert and Yogarany Chelliah and Cécile Frolet and Wilber Quispe-Tintaya and Jules A Hoffmann and Stéphanie A Blandin and Elena A Levashina},
doi = {10.1016/j.chom.2009.01.005},
issn = {1934-6069},
year = {2009},
date = {2009-03-01},
journal = {Cell Host Microbe},
volume = {5},
number = {3},
pages = {273--284},
abstract = {Plasmodium development within Anopheles mosquitoes is a vulnerable step in the parasite transmission cycle, and targeting this step represents a promising strategy for malaria control. The thioester-containing complement-like protein TEP1 and two leucine-rich repeat (LRR) proteins, LRIM1 and APL1, have been identified as major mosquito factors that regulate parasite loads. Here, we show that LRIM1 and APL1 are required for binding of TEP1 to parasites. RNAi silencing of the LRR-encoding genes results in deposition of TEP1 on Anopheles tissues, thereby depleting TEP1 from circulation in the hemolymph and impeding its binding to Plasmodium. LRIM1 and APL1 not only stabilize circulating TEP1, they also stabilize each other prior to their interaction with TEP1. Our results indicate that three major antiparasitic factors in mosquitoes jointly function as a complement-like system in parasite killing, and they reveal a role for LRR proteins as complement control factors.},
keywords = {Animals, Anopheles, APL1, Biological, blandin, Complement System Proteins, Hemolymph, hoffmann, Immunologic Factors, LRIM1, M3i, Models, Plasmodium, Protein Binding, Proteins, TEP1},
pubstate = {published},
tppubtype = {article}
}