GSBS Student Publications

Title

PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Medicine, Division of Infectious Disease and Immunology

Date

6-13-2006

Document Type

Article

Medical Subject Headings

Amino Acid Motifs; Amino Acid Sequence; Animals; Bordetella pertussis; Carrier Proteins; Cell Membrane; Cells, Cultured; Diaminopimelic Acid; Drosophila Proteins; Drosophila melanogaster; Escherichia coli; Gene Expression Regulation; Hemolymph; Intracellular Fluid; Malpighian Tubules; Molecular Sequence Data; Peptide Fragments; Peptidoglycan; RNA Interference; Recombinant Fusion Proteins; Signal Transduction; Transfection; Virulence Factors, Bordetella

Disciplines

Life Sciences | Medicine and Health Sciences

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.

Rights and Permissions

Citation: Nat Immunol. 2006 Jul;7(7):715-23. Epub 2006 Jun 11. Link to article on publisher's site

DOI of Published Version

10.1038/ni1356

Related Resources

Link to article in PubMed

Journal Title

Nature immunology

PubMed ID

16767093