Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan

  • Science. 2003 Jun 6;300(5625):1584-7. doi: 10.1126/science.1084677.
Stephen E Girardin  1 ,  Ivo G Boneca ,  Leticia A M Carneiro ,  Aude Antignac ,  Muguette Jéhanno ,  Jérôme Viala ,  Karsten Tedin ,  Muhamed-Kheir Taha ,  Agnes Labigne ,  Ulrich Zähringer ,  Anthony J Coyle ,  Peter S DiStefano ,  John Bertin ,  Philippe J Sansonetti ,  Dana J Philpott
Affiliations
  • 1. Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Institut Pasteur, 28, Rue du Dr. Roux, 75724Paris Cedex 15, France.
PMID: 12791997 DOI: 10.1126/science.1084677
Abstract

Although the role of Toll-like receptors in extracellular Bacterial sensing has been investigated intensively, intracellular detection of bacteria through Nod molecules remains largely uncharacterized. Here, we show that human NOD1 specifically detects a unique diaminopimelate-containing N-acetylglucosamine-N-acetylmuramic acid (GlcNAc-MurNAc) tripeptide motif found in Gram-negative Bacterial peptidoglycan, resulting in activation of the transcription factor NF-kappaB pathway. Moreover, we show that in epithelial cells (which represent the first line of defense against invasive pathogens), Nod1is indispensable for intracellular Gram-negative Bacterial sensing.