Journal
CHEMBIOCHEM
Volume 14, Issue 4, Pages 482-488Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201200655
Keywords
compound libraries; glycosylation; Nod2; peptidoglycans
Funding
- Japan Society for the Promotion of Science [23.1965, 19310144, 20241053, 22310136]
- Institute for Fermentation, Osaka (IFO)
- Suntory Institute for Bioorganic Research (SUNBOR Grant)
- Houansha Foundation
- Takeda Science Foundation
- Naito Foundation
- Japan Chemical Innovation and Inspection Institute
- Osaka University's Global COE program (Frontier Biomedical Science Underlying Organelle Network Biology)
- JSPS [LR025]
- CSTP
- Grants-in-Aid for Scientific Research [20241053, 19310144, 23241074, 22310136, 21106008] Funding Source: KAKEN
Ask authors/readers for more resources
Nucleotide oligomerization domain-containing protein 2 (Nod2), an innate immune receptor, recognizes bacterial cell-wall peptidoglycan (PGN), the minimum ligand of which is muramyl dipeptide (MDP). Enzymatic digestion of PGN appears to be important for Nod2 recognition. PGN is degraded by muramidase or glucosamidase through a process that produces two types of glycan sequence; glycans containing GlcNAc(14)MurNAc or MurNAc(14)GlcNAc. In this report, a range of disaccharide or tetrasaccharide fragments of each sequence were chemically synthesized, and their activities in stimulating human Nod2 (hNod2) were investigated. The results reveal that hNod2 recognitions is dependent on the glycan sequence, as demonstrated by comparing the activities of glycans with the same peptide moieties. (MurNAc(14)GlcNAc)2-containing structures exhibited stronger activity than those containing (GlcNAc(14)MurNAc)2. The results suggest that differences in the enzymatic degradation process affect the host's immunomodulation process.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available