ArticleInfection and immunity2007
Modification of the structure of peptidoglycan is a strategy to avoid detection by nucleotide-binding oligomerization domain protein 1.
Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 54 citations in OpenAlex.
- Genetic interference of distinctive Mycobacterium tuberculosis peptidoglycan modifications enhances β-lactam susceptibility and reveals expression-sensitive host immune dynamics.Scientific reports · 2026Article
- Exploration of Regulatory Elements, MicroRNAs, and Copy Number Variation in Urogenital Chlamydia Reinfection in African American Women.International journal of molecular sciences · 2026Article
- Compositional analysis of bacterial peptidoglycan: insights from peptidoglycomics into structure and function.Journal of bacteriology · 2025Review
- Mechanisms conferring bacterial cell wall variability and adaptivity.Biochemical Society transactions · 2024Review
- Peptidoglycan from Bacillus anthracis Inhibits Human Macrophage Efferocytosis in Part by Reducing Cell Surface Expression of MERTK and TIM-3.ImmunoHorizons · 2024Article
- Small molecule modulators of immune pattern recognition receptors.RSC chemical biology · 2023Review
- Amidation of glutamate residues in mycobacterial peptidoglycan is essential for cell wall cross-linking.Frontiers in cellular and infection microbiology · 2023Article
- The SGNH hydrolase family: a template for carbohydrate diversity.Glycobiology · 2022Review
- Plant peptidoglycan precursor biosynthesis: Conservation between moss chloroplasts and Gram-negative bacteria.Plant physiology · 2022Article
- Synthesis of Bacterial-Derived Peptidoglycan Cross-Linked Fragments.The Journal of organic chemistry · 2020Article
- Facile Synthesis and Metabolic Incorporation ofACS chemical biology · 2020Article
- Cell wall peptidoglycan in Mycobacterium tuberculosis: An Achilles' heel for the TB-causing pathogen.FEMS microbiology reviews · 2019Review
- Modulation of the NOD-like receptors NOD1 and NOD2: A chemist's perspective.Bioorganic & medicinal chemistry letters · 2019Review
- Translation of peptidoglycan metabolites into immunotherapeutics.Clinical & translational immunology · 2019Review
- Membrane Association Dictates Ligand Specificity for the Innate Immune Receptor NOD2.ACS chemical biology · 2017Article
- The Dual NOD1/NOD2 Agonism of Muropeptides Containing a Meso-Diaminopimelic Acid Residue.PloS one · 2016Article
- Article
- Bacterial interference with canonical NFκB signalling.Microbiology (Reading, England) · 2013Review
- The alternative translational profile that underlies the immune-evasive state of persistence in Chlamydiaceae exploits differential tryptophan contents of the protein repertoire.Microbiology and molecular biology reviews : MMBR · 2012Review
- Identification of genetic determinants and enzymes involved with the amidation of glutamic acid residues in the peptidoglycan of Staphylococcus aureus.PLoS pathogens · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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-alpha) gene expression without significant TNF-alpha 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-alpha protein production. The compounds that induced synergistic effects were also able to activate NF-kappaB in a NOD1- or NOD2-dependent manner, implicating these proteins in synergistic TNF-alpha secretion. It was found that a diaminopimelic acid (DAP)-containing muramyl tetrapeptide could activate NF-kappaB in a NOD1-dependent manner, demonstrating that an exposed DAP is not essential for NOD1 sensing. The activity was lost when the alpha-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 alpha-carboxylic acid of iso-glutamic acid. Many pathogens modify the alpha-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.
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