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...

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

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

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.

scholarly journals CARD6 Is Interferon Inducible but Not Involved in Nucleotide-Binding Oligomerization Domain Protein Signaling Leading to NF-κB Activation

2007 ◽  
Vol 28 (5) ◽  
pp. 1541-1552 ◽  
Author(s):  
Almut Dufner ◽  
Gordon S. Duncan ◽  
Andrew Wakeham ◽  
Alisha R. Elford ◽  
Håkan T. Hall ◽  
...  
Keyword(s):  
Nucleotide Binding ◽  
Adenovirus Type ◽  
Lymphocytic Choriomeningitis ◽  
Immune Defense ◽  
Protein Signaling ◽  
Interacting Protein ◽  
Serovar Typhimurium ◽  
Bacterial Peptidoglycan ◽  
Oligomerization Domain

ABSTRACT We have previously reported the cloning and characterization of CARD6, a caspase recruitment domain (CARD)-containing protein that is structurally related to the interferon (IFN)-inducible GTPases. CARD6 associates with microtubules and with receptor-interacting protein 2 (RIP2). RIP2 mediates NF-κB activation induced by the intracellular nucleotide-binding oligomerization domain (NOD) receptors that sense bacterial peptidoglycan. Here we report that the expression of CARD6 and RIP2 in bone marrow-derived macrophages is rapidly induced by beta IFN and gamma IFN. This IFN-induced upregulation of CARD6 is suppressed by lipopolysaccharide (LPS), in contrast to LPS's enhancement of IFN-induced RIP2 upregulation. We generated CARD6-deficient (CARD6−/−) mice and carried out extensive analyses of signaling pathways mediating innate and adaptive immune responses, including the NOD pathways, but did not detect any abnormalities. Moreover, CARD6−/− mice were just as susceptible as wild-type mice to infection by Salmonella enterica serovar Typhimurium, Listeria monocytogenes, Candida albicans, lymphocytic choriomeningitis virus, or mouse adenovirus type 1. Thus, although structural and in vitro analyses strongly suggest an important role for CARD6 in immune defense, the physiological function of CARD6 remains obscure.

Sign in / Sign up

Export Citation Format

Share Document