PMID:15476918,12351681,9609827,12872120 Activation of theToll transmembrane receptor by its ligand Sp¡¯atzle (SPZ) leads to the formation of a multimeric receptor?adaptor complex, which comprises three death-domain proteins: MyD88, Tube and the kinase Pelle

PMID: 15476918,12123572,12433364,11485985 Activation of this pathway triggers a cascade of kinases (DmTAK, IKK), which ultimately phosphorylates the Rel protein Relish

PMID: 15476918,12732719,11269502 Phosphorylated Relish is then cleaved by the DREDD caspase dissociating the IKappa-B like domain from the Rel DNA binding domain, which can then translocate into the nucleus

PMID: 15476918,12732719,11269502 Phosphorylated Relish is then cleaved by the DREDD caspase dissociating the IKappa-B like domain from the Rel DNA binding domain, which can then translocate into the nucleus

PMID: 15476918,14684822,14722090 These genetic data are correlated with biochemical studies indicating that PGRP-SA and GNBP-1 could be part of the same protein complex PMID:15476918 These genetic data, combined with the known ability of PGRP-SA to bind PGN, make PGRPSA a bona fide PRRs upstream of the Toll pathway

PMID: 15476918 First, LTA is also a PGRP-SA/GNBP-1-dependent elicitor of the Toll pathway, suggesting that the same receptor or receptor complex can detect multiple PAMPs

PMID:15476918,11106397 Using RNA interference to knock down specific isoforms, Werner et al. showed that the x isoform is the only one required for diptericin induction by DAP-PGN PMID: 15476918 Another member of the PGRP family, PGRP-LE could be a potential partner for PGRP-LC in Gram-negative sensing.

PMID:15476918,11106397 On the contrary, response to LPS could involve a cooperation between PGRP-LCx and PGRP-LCa PMID: 15476918 Another member of the PGRP family, PGRP-LE could be a potential partner for PGRP-LC in Gram-negative sensing.

PMID:15476918 Abroader binding specificitywas also reported for Holotrichia diomphalia PGRP-1 and PGRP-2 that bind to both PGN and Beta1,3-glucan.

PMID:15476918 Abroader binding specificitywas also reported for Holotrichia diomphalia PGRP-1 and PGRP-2 that bind to both PGN and Beta1,3-glucan.

PMID:15476918,12351681,9609827,12872120 Activation of theToll transmembrane receptor by its ligand Sp¡¯atzle (SPZ) leads to the formation of a multimeric receptor?adaptor complex, which comprises three death-domain proteins: MyD88, Tube and the kinase Pelle

PMID:15476918 Abroader binding specificitywas also reported for Holotrichia diomphalia PGRP-1 and PGRP-2 that bind to both PGN and Beta1,3-glucan.

PMID:15476918 Abroader binding specificitywas also reported for Holotrichia diomphalia PGRP-1 and PGRP-2 that bind to both PGN and Beta1,3-glucan.

PMID: 15476918,8755572 The C-terminal part of B. mori GNBP has a strong specificity and high affinity for Beta1,3-glucan and for LPS PMID: 15476918,10671539 The N-terminal 100 AA, known as the GNBP homology domain, can also bind Beta1,3-glucan

PMID: 15476918,8755572 The C-terminal part of B. mori GNBP has a strong specificity and high affinity for Beta1,3-glucan and for LPS

PMID: 15476918 In most insects, these proteins are involved in LPS and Beta1,3-glucan-dependent activation of the protease cascades leading to prophenoloxidase activation.

PMID: 15476918 In most insects, these proteins are involved in LPS and Beta1,3-glucan-dependent activation of the protease cascades leading to prophenoloxidase activation.

PMID: 15476918 In most insects, these proteins are involved in LPS and Beta1,3-glucan-dependent activation of the protease cascades leading to prophenoloxidase activation.

PMID: 15476918,14684822,14722090 These genetic data are correlated with biochemical studies indicating that PGRP-SA and GNBP-1 could be part of the same protein complex PMID:15476918 These genetic data, combined with the known ability of PGRP-SA to bind PGN, make PGRPSA a bona fide PRRs upstream of the Toll pathway

PMID: 15476918 GNBP- 1 overexpression in Drosophila cell culture increases AMP gene transcription after stimulation by LPS or Beta1,3-glucan

PMID: 15476918 GNBP- 1 overexpression in Drosophila cell culture increases AMP gene transcription after stimulation by LPS or Beta1,3-glucan

PMID:15476918,12351681,9609827,12872120 Activation of theToll transmembrane receptor by its ligand Sp¡¯atzle (SPZ) leads to the formation of a multimeric receptor?adaptor complex, which comprises three death-domain proteins: MyD88, Tube and the kinase Pelle

PMID: 15476918,9326640,12225919 While this discrepancy will need furtherwork to be understood, it should be noted that mosquito GNBP recognizes both Gram-positive and Gram-negative bacteria when overexpressed in culture cells and that some Manduca sexta BetaGRPs can bind simultaneously LPS and LTA

PMID: 15476918 One possible model could be that, in Drosophila, PGN and LTA are recognized respectively by PGRP-SA and GNBP-1

PMID: 15476918 One possible model could be that, in Drosophila, PGN and LTA are recognized respectively by PGRP-SA and GNBP-1

PMID: 15476918,12225919 Its (hemolin) recognition specificity ranges from LTA to LPS and Beta1,3- glucan

PMID: 15476918,12225919 Its (hemolin) recognition specificity ranges from LTA to LPS and beta1,3- glucan

PMID: 15476918,12225919 Its (hemolin) recognition specificity ranges from LTA to LPS and beta1,3- glucan

PMID: 15476918,10954704 C-type lectins form an important class of calcium-dependent carbohydrate-binding proteins implicated in both vertebrate and invertebrate innate immune responses. Composed of one or more carbohydrate recognition domains, these proteins are found in lepidopteran plasma where, as described below, they are necessary for LPS-mediated proPO activation

PMID: 15476918,10954704 C-type lectins form an important class of calcium-dependent carbohydrate-binding proteins implicated in both vertebrate and invertebrate innate immune responses. Composed of one or more carbohydrate recognition domains, these proteins are found in lepidopteran plasma where, as described below, they are necessary for LPS-mediated proPO activation

PMID: 15476918,10954704 Composed of one or more carbohydrate recognition domains, these proteins are found in lepidopteran plasma where, as described below, they are necessary for LPS-mediated proPO activation

PMID: 15476918 A proposed model would be that SPH bound to Immunolectin-2 would recruit proPO and PPAE at the site of infection

PMID:15476918 Assembly of these proteins as a complex induces phosphorylation of the IKappa-B like inhibitor Cactus by an unknown kinase distinct from Pelle. Phosphorylated cactus is degraded by the proteasome and dissociates from the Rel transcription factor dorsal-related immunity factor (DIF) that is then free to translocate into the nucleus and to activate numerous genes, including AMP genes.

PMID: 15476918 A proposed model would be that SPH bound to Immunolectin-2 would recruit proPO and PPAE at the site of infection

PMID;15476918,11912489 dSR-CI, another Drosophila scavenger receptor (SR), is macrophage specific and recognizes a broad range of polyanionic ligands much like the mammalian class A SR

PMID:15476918 Assembly of these proteins as a complex induces phosphorylation of the IKappa-B like inhibitor Cactus by an unknown kinase distinct from Pelle. Phosphorylated cactus is degraded by the proteasome and dissociates from the Rel transcription factor dorsal-related immunity factor (DIF) that is then free to translocate into the nucleus and to activate numerous genes, including AMP genes.

PMID:15476918 Assembly of these proteins as a complex induces phosphorylation of the IKappa-B like inhibitor Cactus by an unknown kinase distinct from Pelle. Phosphorylated cactus is degraded by the proteasome and dissociates from the Rel transcription factor dorsal-related immunity factor (DIF) that is then free to translocate into the nucleus and to activate numerous genes, including AMP genes.

PMID:15476918 Assembly of these proteins as a complex induces phosphorylation of the IKappa-B like inhibitor Cactus by an unknown kinase distinct from Pelle. Phosphorylated cactus is degraded by the proteasome and dissociates from the Rel transcription factor dorsal-related immunity factor (DIF) that is then free to translocate into the nucleus and to activate numerous genes, including AMP genes.

PMID:15476918 Assembly of these proteins as a complex induces phosphorylation of the IKappa-B like inhibitor Cactus by an unknown kinase distinct from Pelle. Phosphorylated cactus is degraded by the proteasome and dissociates from the Rel transcription factor dorsal-related immunity factor (DIF) that is then free to translocate into the nucleus and to activate numerous genes, including AMP genes.