期刊
ACS INFECTIOUS DISEASES
卷 3, 期 4, 页码 264-270出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsinfecdis.6b00154
关键词
nucleotide-binding oligomerization domain-containing 2; muramyl dipeptide; peptidoglycan; innate immunity; leucine-rich repeat domain; surface plasmon resonance
资金
- Delaware COBRE program
- National Institute of General Medical Sciences from the National Institutes of Health [NIGMS 1 P30 GM110758, 1 P20 GM104316-01A1]
- Pew Charitable Trusts
- National Science Foundation [CAREER CHE 1554967]
- NIH through a CBI training grant [5T32GM008550]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1554967] Funding Source: National Science Foundation
Genetic mutations in the innate immune receptor nucleotide-binding oligomerization domain-containing 2 (Nod2) have demonstrated increased susceptibility to Crohn's disease, an inflammatory bowel disease that is hypothesized to be accompanied by changes in the gut microbiota. Nod2 responds to the presence of bacteria, specifically a fragment of the bacterial cell wall, muramyl dipeptide (MDP). The proposed site of this interaction is the leucine-rich repeat (LRR) domain. Surface plasmon resonance and molecular modeling were used to investigate the interaction of the LRR domain with MDP. A functional and pure LRR domain was obtained from Escherichia coli expression in high yield. The LRR domain binds to MDP with high affinity, with a K-D of 212 +/- 24 nM. Critical portions of the receptor were determined by mutagenesis of putative binding residues. Fragment analysis of MDP revealed that both the peptide and carbohydrate portion contribute to the binding interaction.
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