Freund's adjuvant, NOD2 and mycobacteria.

Abstract

PURPOSE:

Mycobacterium tuberculosis contributed to the discovery of delayed-type hypersensitivity and cell-mediated immunity. However, the biochemical basis for the immunogenicity of the mycobacterial cell wall has until recently remained unknown.

RECENT FINDINGS:

Nucleotide-binding oligomerization domain-containing protein 2 (NOD2) responds to bacterial peptidolycan-derived muramyl dipeptide (MDP). Whereas most bacteria produce N-acetyl MDP, mycobacteria produce an unusual modified form of MDP, called N-glycolyl MDP. Disruption of N-glycolyl MDP synthesis in mycobacteria greatly diminishes the contribution of NOD2 to mycobacterial sensing. Additionally, N-glycolyl MDP is more potent and efficacious than N-acetyl MDP at inducing innate responses and T cell-mediated immunity.

SUMMARY:

The sensitivity of NOD2 to the mycobacterial peptidoglycan may link the natural history of both innate and adaptive immunity to mycobacterial infection.

• Authors: Marcel A Behr, Maziar Divangahi
• Journal: Current opinion in microbiology (Curr Opin Microbiol) Vol. 23 Pg. 126-32 (Feb 2015) ISSN: 1879-0364 [Electronic] England
• PMID: 25483349 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
• Copyright: Copyright © 2014 Elsevier Ltd. All rights reserved.

Chemical References

• NOD2 protein, human
• Nod2 Signaling Adaptor Protein
• Peptidoglycan
• Acetylmuramyl-Alanyl-Isoglutamine
• Freund's Adjuvant

Topics

• Acetylmuramyl-Alanyl-Isoglutamine (immunology, metabolism)
• Cell Wall (immunology, metabolism)
• Freund's Adjuvant (metabolism)
• Immunity, Innate
• Mycobacterium tuberculosis (immunology)
• Nod2 Signaling Adaptor Protein (metabolism)
• Peptidoglycan (immunology, metabolism)
• T-Lymphocytes (immunology)