학술논문

An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid.
Document Type
Article
Source
Nature Immunology. Jul2003, Vol. 4 Issue 7, p702. 6p.
Subject
*NUCLEOTIDES
*PROTEINS
*PEPTIDOGLYCANS
*GRAM-negative bacteria
*MACROPHAGES
Language
ISSN
1529-2908
Abstract
Nucleotide-binding oligomerization domain protein 1 (NOD1) belongs to a family that includes multiple members with NOD and leucine-rich repeats in vertebrates and plants. NOD1 has been suggested to have a role in innate immune responses, but the mechanism involved remains unknown. Here we report that NOD1 mediates the recognition of peptidoglycan derived primarily from Gram-negative bacteria. Biochemical and functional analyses using highly purified and synthetic compounds indicate that the core structure recognized by NOD1 is a dipeptide, γ-D-glutamyl-meso-diaminopimelic acid (iE-DAP). Murine macrophages deficient in NOD1 did not secrete cytokines in response to synthetic iE-DAP and did not prime the lipopolysaccharide response. Thus, NOD1 mediates selective recognition of bacteria through detection of iE-DAP-containing peptidoglycan. [ABSTRACT FROM AUTHOR]