scholarly journals Muramyl dipeptide activation of nucleotide-binding oligomerization domain 2 protects mice from experimental colitis

2008 ◽  
Author(s):  
Tomohiro Watanabe ◽  
Naoki Asano ◽  
Peter J. Murray ◽  
Keiko Ozato ◽  
Prafullakumar Tailor ◽  
...  
Keyword(s):  
Muramyl Dipeptide ◽  
Experimental Colitis ◽  
Nucleotide Binding ◽  
Oligomerization Domain

96 Muramyl Dipeptide Activation of Nucleotide-Binding Oligomerization Domain 2 Protects Mice from Experimental Colitis

2008 ◽  
Vol 134 (4) ◽  
pp. A-16 ◽  
Author(s):  
Tomohiro Watanabe ◽  
Naoki Asano ◽  
Peter Murray ◽  
Keiko Ozato ◽  
Atsushi Kitani ◽  
...  
Keyword(s):  
Muramyl Dipeptide ◽  
Experimental Colitis ◽  
Nucleotide Binding ◽  
Oligomerization Domain

scholarly journals Modification of the Structure of Peptidoglycan Is a Strategy To Avoid Detection by Nucleotide-Binding Oligomerization Domain Protein 1

2006 ◽  
Vol 75 (2) ◽  
pp. 706-713 ◽  
Author(s):  
Margreet A. Wolfert ◽  
Abhijit Roychowdhury ◽  
Geert-Jan Boons
Keyword(s):  
Carboxylic Acid ◽  
Glutamic Acid ◽  
Synergistic Effects ◽  
Muramyl Dipeptide ◽  
Nucleotide Binding ◽  
Diaminopimelic Acid ◽  
Dependent Manner ◽  
Necrosis Factor Alpha ◽  
Tnf Α ◽  
Oligomerization Domain

ABSTRACT Nucleotide-binding oligomerization domain (NOD) protein 1 (NOD1) and NOD2 are pathogen recognition receptors that sense breakdown products of peptidoglycan (PGN) (muropeptides). It is shown that a number of these muropeptides can induce tumor necrosis factor alpha (TNF-α) gene expression without significant TNF-α translation. This translation block is lifted when the muropeptides are coincubated with lipopolysaccharide (LPS), thereby accounting for an apparently synergistic effect of the muropeptides with LPS on TNF-α protein production. The compounds that induced synergistic effects were also able to activate NF-κB in a NOD1- or NOD2-dependent manner, implicating these proteins in synergistic TNF-α secretion. It was found that a diaminopimelic acid (DAP)-containing muramyl tetrapeptide could activate NF-κB in a NOD1-dependent manner, demonstrating that an exposed DAP is not essential for NOD1 sensing. The activity was lost when the α-carboxylic acid of iso-glutamic acid was modified as an amide. However, agonists of NOD2, such as muramyl dipeptide and lysine-containing muramyl tripeptides, were not affected by amidation of the α-carboxylic acid of iso-glutamic acid. Many pathogens modify the α-carboxylic acid of iso-glutamic acid of PGN, and thus it appears this is a strategy to avoid recognition by the host innate immune system. This type of immune evasion is in particular relevant for NOD1.

scholarly journals Pathogen Sensing by Nucleotide-binding Oligomerization Domain-containing Protein 2 (NOD2) Is Mediated by Direct Binding to Muramyl Dipeptide and ATP

2012 ◽  
Vol 287 (27) ◽  
pp. 23057-23067 ◽  
Author(s):  
Jinyao Mo ◽  
Joseph P. Boyle ◽  
Christopher B. Howard ◽  
Tom P. Monie ◽  
Beckley K. Davis ◽  
...  
Keyword(s):  
Muramyl Dipeptide ◽  
Nucleotide Binding ◽  
Direct Binding ◽  
Oligomerization Domain

Identification of MDP (muramyl dipeptide)-binding key domains in NOD2 (nucleotide-binding and oligomerization domain-2) receptor of Labeo rohita

2012 ◽  
Vol 39 (4) ◽  
pp. 1007-1023 ◽  
Author(s):  
Jitendra Maharana ◽  
Banikalyan Swain ◽  
Bikash R. Sahoo ◽  
Manas R. Dikhit ◽  
Madhubanti Basu ◽  
...  
Keyword(s):  
Labeo Rohita ◽  
Muramyl Dipeptide ◽  
Nucleotide Binding ◽  
Oligomerization Domain

Mannosylated adamantane-containing desmuramyl peptide recognition by NOD2 receptor: a molecular dynamics study

2021 ◽  
Author(s):  
Aleksandra Maršavelski ◽  
Marija Paurević ◽  
Rosana Ribic
Keyword(s):  
Molecular Dynamics ◽  
Muramyl Dipeptide ◽  
Nucleotide Binding ◽  
Peptide Recognition ◽  
Intracellular Receptor ◽  
Bacterial Peptidoglycan ◽  
Oligomerization Domain

Nucleotide-binding oligomerization domain 2 (NOD2) is an intracellular receptor that recognizes the bacterial peptidoglycan fragment, muramyl dipeptide (MDP). Our group has synthesized and biologically evaluated desmuramyl peptides containing adamantane and...

A Novel X-Linked Inhibitor of Apoptosis Deficient Variant Showing Attenuated Epstein-Barr Virus Response

2020 ◽  
Author(s):  
Youjia Zhong ◽  
Chiung-Hui Huang ◽  
Win Mar Soe ◽  
Koon Wing Chan ◽  
Mas Suhaila Isa ◽  
...  
Keyword(s):  
Hemophagocytic Lymphohistiocytosis ◽  
Epstein Barr Virus ◽  
Virus Disease ◽  
Muramyl Dipeptide ◽  
Nucleotide Binding ◽  
Inhibitor Of Apoptosis ◽  
Barr Virus ◽  
Epstein Barr ◽  
Oligomerization Domain

Abstract We report on 2 Asian siblings with X-linked inhibitor of apoptosis deficiency that arose from a novel deletion that presented with Epstein-Barr virus disease and hemophagocytic lymphohistiocytosis. This disease is ascribed to dysfunction in the nucleotide binding and oligomerization domain receptor pathway, tested using a modified muramyl dipeptide–mediated assay.

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