Processing of Bacillus subtilis peptidoglycan by a mouse macrophage cell line

Vermeulen, Mary W.; Gray, Gary R.

doi:10.1128/iai.46.2.476-483.1984

Cited by 60 publications

(24 citation statements)

References 20 publications

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“…Studies clearly show M‐TriDAP to be a specific NOD1 agonist in the 293 cell system 3, 11, 16. The existence of a further enzyme capable of hydrolysis of the D‐isoGln‐ meso ‐DAP acid bond has been suggested by radio‐labelled studies of peptidoglycan processing in macrophages 25, 26. In bacteria, the p60 family of endopeptidases performs this function 27, and although an equivalent eukaryotic enzyme has not yet been described, similar differential expression of such an enzyme in leukocytes and 293 cells (as seen for the two known eukaryotic peptidoglycan processing enzymes) seems likely to explain the differences observed in our study between M‐TriDAP and Tri‐DAP/FK565.…”

Section: Discussionmentioning

confidence: 96%

Normal responses to specific NOD1‐activating peptidoglycan agonists in the presence of the NOD2 frameshift and other mutations in Crohn's disease

Heel¹,

Hunt²,

Ghosh³

et al. 2006

Eur J Immunol

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Both NOD2/CARD15 alleles are mutatedin *10% of Crohn's disease patients, causing loss of functional responses to low-dose muropeptide agonists. We hypothesized that NOD2 mutations may also impair NOD1/CARD4 responses, supported by data suggesting NOD2 1007fs/1007fs patients had reduced responses to a putative NOD1 agonist, diaminopimelic acid-containing muramyl tripeptide (M-TriDAP). We measured peripheral blood mononuclear cell (n = 8 NOD2 wild type, n = 4 1007fs/1007fs, n = 6 702Trp/1007fs, n = 5 702Trp/702Trp, n = 3 908Arg/1007fs) responses to NOD1 agonists alone (IL-8/TNF-a), and agonist enhancement of lipopolysaccharide (LPS) responses (IL-1b).Significant responseswereseenwithM-TriDAPat10 nM (as withNOD2 agonists), but only at !100 nM with FK565/TriDAP. M-TriDAP induced IL-8/TNF-a secretion, and enhancement of LPS IL-1b responses was significantly reduced between NOD2 double mutation carriers versus healthy controls, whereas there was no difference with FK565 or TriDAP stimulation, or between 1007fs/1007fs cells and other genotypes. M-TriDAP contains both NOD1 (c-D-Glu-mesoDAP) and NOD2 (MurNAc-L-Ala-D-Glu) minimal structures whereas FK565/TriDAP contain only NOD1 activating structures. M-TriDAP has dual NOD1/NOD2 agonist activity in primary cells, possibly due to different intracellular peptidoglycan processing compared to the HEK293 cell system typically used for agonist specificity studies. Responses to specific NOD1 agonists are unaffected by NOD2 genotype, suggesting independent action of the NOD1 and NOD2 pathways.

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Section: Discussionmentioning

confidence: 96%

Normal responses to specific NOD1‐activating peptidoglycan agonists in the presence of the NOD2 frameshift and other mutations in Crohn's disease

Heel¹,

Hunt²,

Ghosh³

et al. 2006

Eur J Immunol

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“…At present, we can only speculate about the source or mechanism of cell entry of MDP or related muropeptides, which activate Nod2. One source might be from phagocytosed bacteria, which have undergone degradation within a phagocytic vacuole [37,38]. However, it is important to recall that Fig.…”

Section: Discussionmentioning

confidence: 99%

MDP-induced interleukin-1β processing requires Nod2 and CIAS1/NALP3

Pan

Mathison

Fearns

et al. 2007

Journal of Leukocyte Biology

129

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Nucleotide-binding oligomerization domain (Nod)2 is a sensor of muramyl dipeptides (MDP) derived from bacterial peptidoglycan. Nod2 also plays a role in some autoinflammatory diseases. Cold-induced autoinflammatory syndrome 1 (CIAS1)/NACHT domain, leucine-rich repeat, and pyrin domain-containing protein 3 (NALP3) has been suggested to be sufficient for MDP-dependent release of mature IL-1beta, but the role of Nod2 in this process is unclear. Using mice bearing selective gene deletions, we provide in vitro and in vivo data showing that MDP-induced IL-1beta release requires Nod2 and CIAS1/NALP3 as well as receptor-interacting protein-2 (Rip2), apoptosis-associated speck-like protein containing a caspase activation and recruitment domain (ASC), and caspase-1. In contrast, MDP-dependent IL-6 production only requires Nod2 and Rip2. Together, our data provide a new understanding of this important pathway of IL-1beta production and allow for further studies of the role of these proteins within the broader context of inflammatory disease.

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“…These findings, however, were not supported by Fox & Fox (1991) as they were unable to detect MP in normal rabbit serum, even though the most sensitive procedure for muramic acid analysis was used. Although it remains to be determined how bacterial cell walls are processed in vivo, cells of the monocyte-macrophage system are known to phagocytize invading bacteria, and the ability of a macrophage cell line to digest Bacillus subtilis CWF into monomeric MPs has been demonstrated earlier ( Vermeulen & Gray 1984).…”

Section: Presence Of Pg-ps In Tissuesmentioning

confidence: 99%

Are Intestinal bacteria involved in the etiology of rheumatoid arthritis?

Hazenberg

Klasen

Kool

et al. 1992

APMIS

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Are intestinal bacteria involved in the etiology of rheumatoid arthritis? APMIS 100: 1-9, 1992. Observations in bowel-related joint diseases give support to this hypothesis. In Crohn's disease and ulcerative colitis, the bowel wall inflammation is complicated in about 20% of the patients by joint inflammation. Bowel infection by Sulmonellu, Shigellu and Yersiniu can provoke joint inflammation and supports an etiological link between bowel bacteria and arthritis. The arthropathic properties of the most abundant group of intestinal bacteria, i.e. the obligate anaerobic bacteria, were studied in an animal model. Cell wall fragments (CWF), with peptidoglycan as the major component, from some Eubacterium and Bijidobacterium species induced a severe chronic polyarthritis in Lewis rats after a single intraperitoneal injection. Eubacterium was found in numbers of 108-109 per gram in stools of healthy subjects and rheumatoid arthritis (RA) patients. CWF of isolated strains of E. uerofuciens were arthropathic. Soluble peptidoglycan polysaccharide complexes (PG-PS) originating from the obligate anaerobic flora were purified from human intestinal contents. PG-PS from ileostomy fluid that proved to be less processed by intestinal enzymes induced chronic arthritis in rats after a single administration in oil in the base of the tail. It was concluded that the human intestinal bowel contains soluble bacterial cell wall products that are arthropathic in an animal model. Peptidoglycan (PG) or its subunits was reported to be present in mammalian tissues. Immunohistochemical studies from our group showed the presence of intestinal PG-PS in sections of normal rat spleen. Bacterial cell wall or PG-induced joint inflammation in rats is proven to be absolutely dependent on functional T cells. T-cell lines were isolated from the lymph nodes of rats with an E. aerofaciens CWF arthritis. A helper T-cell line B13 was in vivo arthritogenic in knee or ankle joints upon intravenous injection in rats and proliferated in vitro on syngeneic spleen cells alone, but was additionally stimulated by intestinal PG-PS and E. uerofaciens CWF. It was postulated that the arthritogenic T cells that seem to be autoreactive are, in fact, recognizing bacterial PG-PS on antigen-presenting cells (APC). It is generally accepted that RA is a T-cell-dependent process and that therefore the reaction is directed at small peptides bound by the major histocompatibility complex of APC. The only peptides present in arthritis inducing intestinal PG-PS and in CWF are PG peptides interlinking the sugar chains. We feel that the immunoreaction against PG peptides plays a pivotal role in experimental and human arthritis of an unknown etiology.

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Processing of Bacillus subtilis peptidoglycan by a mouse macrophage cell line

Cited by 60 publications

References 20 publications

Normal responses to specific NOD1‐activating peptidoglycan agonists in the presence of the NOD2 frameshift and other mutations in Crohn's disease

Normal responses to specific NOD1‐activating peptidoglycan agonists in the presence of the NOD2 frameshift and other mutations in Crohn's disease

MDP-induced interleukin-1β processing requires Nod2 and CIAS1/NALP3

Are Intestinal bacteria involved in the etiology of rheumatoid arthritis?

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