Ligand-induced Dimerization of Drosophila Peptidoglycan Recognition Proteins in Vitro

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2005 Apr 22

PMID 15843462

Citations 31

Authors

Peter Mellroth

Jenny Karlsson

Janet Hakansson

Niklas Schultz

William E Goldman

Hakan Steiner

Affiliations

Soon will be listed here.

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.

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