ArticleJournal of the American Chemical Society2020
Differential Peptidoglycan Recognition Assay Using Varied Surface Presentations.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Review
- Probenecid relieves LPS-induced neuroinflammation by modulating the NLRP1 inflammasome pathway in BV2 cells.Scientific reports · 2025Article
- Chemical tools to study and modulate glycan-mediated host-bacteria interactions.Current opinion in chemical biology · 2025Review
- Synthesis of aMolecules (Basel, Switzerland) · 2024Article
- Structure-activity relationship in NOD2 agonistic muramyl dipeptides.European journal of medicinal chemistry · 2024Review
- Small molecule modulators of immune pattern recognition receptors.RSC chemical biology · 2023Review
- Purinergic neurotransmission receptor P2X4 silencing alleviates intracerebral hemorrhage-induced neuroinflammation by blocking the NLRP1/Caspase-1 pathway.Scientific reports · 2023Article
- Article
- Application of bioanalytical and computational methods in decoding the roles of glycans in host-pathogen interactions.Current opinion in chemical biology · 2023Review
- Article
- Purification and Characterization of a Stable, Membrane-Associated Peptidoglycan Responsive Adenylate Cyclase LRR Domain from Human CommensalBiochemistry · 2022Article
- Customized peptidoglycan surfaces to investigate innate immune recognition via surface plasmon resonance.Methods in enzymology · 2022Article
- The Roles of Neutrophils in Cytokine Storms.Viruses · 2021Review
- Bacterial Peptidoglycan Fragments Differentially Regulate Innate Immune Signaling.ACS central science · 2021Article
- Synthesis of Bacterial-Derived Peptidoglycan Cross-Linked Fragments.The Journal of organic chemistry · 2020Article
- Revisiting peptidoglycan sensing: interactions with host immunity and beyond.Chemical communications (Cambridge, England) · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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, which will be critical information to manipulate these responses and combat diseases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.