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Proc Natl Acad Sci U S A. 2005 May 3;102(18):6455-60. Epub 2005 Apr 20.

Ligand-induced dimerization of Drosophila peptidoglycan recognition proteins in vitro.

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  • 1Department of Genetics, Microbiology, and Toxicology, University of Stockholm, S-106 91 Stockholm, Sweden.

Abstract

Drosophila knockout mutants have placed peptidoglycan recognition proteins (PGRPs) in the two major pathways controlling immune gene expression. We now examine PGRP affinities for peptidoglycan. PGRP-SA and PGRP-LCx are bona fide pattern recognition receptors, and PGRP-SA, the peptidoglycan receptor of the Toll/Dif pathway, has selective affinity for different peptidoglycans. PGRP-LCx, the default peptidoglycan receptor of the Imd/Relish pathway, has strong affinity for all polymeric peptidoglycans tested and for monomeric peptidoglycan. PGRP-LCa does not have affinity for polymeric or monomeric peptidoglycan. Instead, PGRP-LCa can form heterodimers with LCx when the latter is bound to monomeric peptidoglycan. Hence, PGRP-LCa can be said to function as an adaptor, thus adding a new function to a member of the PGRP family.

PMID:
15843462
[PubMed - indexed for MEDLINE]
PMCID:
PMC1088352
Free PMC Article
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