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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:15476918,12351681,9609827,12872120
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:15476918,12351681,9609827,12872120
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
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.
indirect
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.
indirect
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.
indirect
PMID: 15476918,12123572,12433364,11485985
Activation of this pathway triggers a
cascade of kinases (DmTAK, IKK), which ultimately phosphorylates
the Rel protein Relish
indirect
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
indirect
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.
indirect
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
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
indirect
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.
indirect
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.
indirect
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
indirect
PMID: 15476918
GNBP-
1 overexpression in Drosophila cell culture increases AMP
gene transcription after stimulation by LPS or Beta1,3-glucan
indirect
PMID: 15476918
GNBP-
1 overexpression in Drosophila cell culture increases AMP
gene transcription after stimulation by LPS or Beta1,3-glucan
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
indirect
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
indirect
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
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
indirect