Differential Peptidoglycan Recognition Assay Using Varied Surface Presentations.

Journal of the American Chemical Society
Elizabeth A D'AmbrosioCatherine L Grimes

Abstract

Bacterial peptidoglycan (PG) is recognized by the human innate immune system to generate an appropriate response. To gain an appreciation of how this essential polymer is sensed, a surface plasmon resonance (SPR) assay using varied PG surface presentation was developed. PG derivatives were synthesized and immobilized on the surface at different positions on the molecule to assess effects of ligand orientation on the binding affinities of NOD-like receptors (NLRs). NLRP1 and NOD2 are cytosolic innate immune proteins known to generate an immune response to PG. Both possess conserved leucine rich repeat domains (LRR) as proposed sites of molecular recognition, though limited biochemical evidence exists regarding the mechanisms of PG recognition. Here direct biochemical evidence for the association of PG fragments to NOD2 and NLRP1 with nanomolar affinity is shown. The orientations in which the fragments were presented on the SPR surface influenced the strength of PG recognition by both NLRs. This assay displays fundamental differences in binding preferences for PG by innate immune receptors and reveals unique recognition mechanisms between the LRRs. Each receptor uses specific ligand structural features to achieve optimal binding,...Continue Reading

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Citations

Oct 16, 2020·Chemical Communications : Chem Comm·Geneva Maddison CrumpCatherine L Grimes
Jun 8, 2021·Organic & Biomolecular Chemistry·Aleksandra MaršavelskiRosana Ribić
Jun 1, 2021·ACS Central Science·Klare L BerschCatherine L Grimes
Oct 28, 2020·The Journal of Organic Chemistry·Siavash MashayekhCatherine L Grimes
Oct 22, 2021·Chemical Research in Toxicology·Peng-Fei Zhao, Zai-Qun Liu
Nov 28, 2021·Viruses·Lily ChanKhalil Karimi

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