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Nod2 Is a General Sensor of Peptidoglycan through Muramyl Dipeptide (MDP) Detection

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Girardin, Stephen E., Boneca, Ivo G., Viala, Jérôme, Chamaillard, Mathias, Labigne, Agnès, Thomas, Gilles, Philpott, Dana J., Sansonetti, Philippe J.·2003·Journal of Biological Chemistry

Abstract

Nod2 activates the NF-kappaB pathway following intracellular stimulation by bacterial products. Recently, mutations in Nod2 have been shown to be associated with Crohn's disease, suggesting a role for bacteria-host interactions in the etiology of this disorder. We show here that Nod2 is a general sensor of peptidoglycan through the recognition of muramyl dipeptide (MDP), the minimal bioactive peptidoglycan motif common to all bacteria. Moreover, the 3020insC frameshift mutation, the most frequent Nod2 variant associated with Crohn's disease patients, fully abrogates Nod2-dependent detection of peptidoglycan and MDP. Together, these results impact on the understanding of Crohn's disease development. Additionally, the characterization of Nod2 as the first pathogen-recognition molecule that detects MDP will help to unravel the well known biological activities of this immunomodulatory compound.

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Crossref · 10.1074/jbc.c200651200

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Metadata

Authors
Girardin, S. E., Boneca, I. G., Viala, J., Chamaillard, M., Labigne, A., Thomas, G., Philpott, D. J., & Sansonetti, P. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-03
Volume
278
Issue
11
Pages
8869-8872
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2075583035
Cited by
2,408
References
2
FWCI
44.30
Type
journal article
Language
en
Open access
hybrid

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