RRC ID 11570
Author Kaneko T, Yano T, Aggarwal K, Lim JH, Ueda K, Oshima Y, Peach C, Erturk-Hasdemir D, Goldman WE, Oh BH, Kurata S, Silverman N.
Title PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan.
Journal Nat. Immunol.
Abstract Drosophila rely entirely on an innate immune response to combat microbial infection. Diaminopimelic acid-containing peptidoglycan, produced by Gram-negative bacteria, is recognized by two receptors, PGRP-LC and PGRP-LE, and activates a homolog of transcription factor NF-kappaB through the Imd signaling pathway. Here we show that full-length PGRP-LE acted as an intracellular receptor for monomeric peptidoglycan, whereas a version of PGRP-LE containing only the PGRP domain functioned extracellularly, like the mammalian CD14 molecule, to enhance PGRP-LC-mediated peptidoglycan recognition on the cell surface. Interaction with the imd signaling protein was not required for PGRP-LC signaling. Instead, PGRP-LC and PGRP-LE signaled through a receptor-interacting protein homotypic interaction motif-like motif. These data demonstrate that like mammals, drosophila use both extracellular and intracellular receptors, which have conserved signaling mechanisms, for innate immune recognition.
Volume 7(7)
Pages 715-23
Published 2006-7
DOI 10.1038/ni1356
PII ni1356
PMID 16767093
MeSH Amino Acid Motifs Amino Acid Sequence Animals Bordetella pertussis / immunology Carrier Proteins / chemistry Carrier Proteins / genetics Carrier Proteins / physiology* Cell Membrane / immunology Cells, Cultured Diaminopimelic Acid / immunology* Drosophila Proteins / biosynthesis Drosophila Proteins / genetics Drosophila Proteins / physiology Drosophila melanogaster / immunology* Escherichia coli / immunology Gene Expression Regulation Hemolymph / immunology Intracellular Fluid / immunology Malpighian Tubules / immunology Molecular Sequence Data Peptide Fragments / physiology Peptidoglycan / chemistry Peptidoglycan / immunology* RNA Interference Recombinant Fusion Proteins / physiology Signal Transduction / immunology Transfection Virulence Factors, Bordetella / chemistry Virulence Factors, Bordetella / immunology*
IF 21.809
Times Cited 165