Activation of nuclear factor-κB in macrophages by mycoplasmal lipopeptides

Sacht, Gudrun; Märten, Angela; Deiters, Ursula; Jung, Günther; Wingender, Edgar; Mühlradt, Peter F.

doi:10.1002/(sici)1521-4141(199812)28:12<4207::aid-immu4207>3.0.co;2-r

Cited by 37 publications

(33 citation statements)

References 31 publications

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“…29 It was previously reported that M. fermentans cause NF-kB activation in human monocytic cell line and murine macrophages. 5,17,30 In a preliminary study, we found that, in our system, NF-kB was translocated to the nucleus in M. fermentans-infected cells (data not shown).…”

Section: Discussionmentioning

confidence: 59%

Mycoplasma fermentans inhibits tumor necrosis factor α-induced apoptosis in the human myelomonocytic U937 cell line

Gerlic

Horowitz

2004

Cell Death Differ

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Mycoplasma fermentans (M. fermentans) was shown to be involved in the alteration of several eukaryotic cell functions (i.e. cytokine production, gene expression), and was suggested as a causative agent in arthritic diseases involving impaired apoptosis. We investigated whether M. fermentans has a pathogenic potential by affecting tumor necrosis factor (TNF)ainduced apoptosis in the human myelomonocytic U937 cell line. A significant reduction in the TNFa-induced apoptosis (B60%) was demonstrated upon either infection with live M. fermentans or by stimulation with non-live M. fermentans. To investigate the mechanism of M. fermentans antiapoptotic effect, the reduction of mitochondrial transmembrane potential (DW m ) and the protease activity of caspase-8 were measured. In the infected cells, the reduction of DW m was inhibited (B75%), and a B60% reduction of caspase-8 activity was measured. In conclusion, M. fermentans significantly inhibits TNFa-induced apoptosis in U937 cells, and its effect is upstream of the mitochondria and upstream of caspase-8.

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Section: Discussionmentioning

confidence: 59%

Mycoplasma fermentans inhibits tumor necrosis factor α-induced apoptosis in the human myelomonocytic U937 cell line

Gerlic

Horowitz

2004

Cell Death Differ

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“…The mechanisms involved in NO and TNF induction by mycoplasmas are poorly understood. Recently, it was shown that mycoplasma activates the transcription factor NF-B in DMBM-3 macrophage cell line [15] and induces transactivation of NF-B and AP-1 in the Raw 264.7 macrophage cell line [14]. It was also reported that Mycoplasma fermentans induces protein tyrosine phosphorylation [31] and activation of the three subgroups of mitogenactivated protein kinases (MAPKs), ERK 1/2, JNKs, and MAPK p38, and that induction of TNF production by mycoplasma involves the ERK 1/2 and p38 kinases [13].…”

Section: Discussionmentioning

confidence: 99%

“…Its structure was elucidated and it constitutes one of the most potent macrophage stimulators [11] together with a lipopeptide recently isolated from M. hyorhinis membranes [12]. The characterization of mycoplasma-derived lipopeptides brought new insights into the mechanisms of NO and TNF induction in macrophages stimulated with mycoplasmas [13][14][15].…”

Section: Introductionmentioning

confidence: 99%

Mycoplasma arginini enhances cytotoxicity of thioglycollate-elicited murine macrophages toward YAC-1 tumor cells through production of NO

Ribeiro‐Dias

Russo

Barbuto

et al. 1999

Journal of Leukocyte Biology

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Bacterial products stimulate macrophage tumoricidal activity through release of tumor necrosis factor (TNF) and nitric oxide (NO). We show here that thioglycollate-elicited macrophages acquire cytotoxic activity when cocultured with Mycoplasma arginini-infected YAC-1 tumor cells and release TNF and NO. Fixed mycoplasmainfected cells, supernatants from infected-cell cultures, or purified heat-killed mycoplasma obtained from cell-free cultures were all able to induce TNF and NO production. Thus, the mycoplasma per se and not a product of infected cells induce the release of these molecules. Addition of prostaglandin E 2 (PGE 2 ) to the cocultures, which reduced TNF release, or antibodies to TNF, did not affect macrophage cytotoxicity nor NO release. Inhibition of NO production by L-NAME or aminoguanidine reduced the cytotoxicity, and treatment with a NO donor was toxic to YAC-1 cells. These results indicate that M. arginini activates thioglycollateelicited murine macrophages for NO and TNF release increasing their cytotoxic activity toward YAC-1 cells and that this activity is dependent on NO but not TNF release. J. Leukoc. Biol. 65: 808-814; 1999.

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“…Tripalmitoyl-S-glyceryl cysteine (Pam3Cys) is a synthetic version of the N-terminal moiety of Braun's lipoprotein that spans the inner and outer membranes of Gram-negative bacteria and has been shown to be capable of stimulating virus-specific CTL responses against influenza virus-infected cells (21) and to elicit protective Abs against foot-and-mouth disease (17) when coupled to the appropriate synthetic epitopes. Recently dipalmitoyl-S-glyceryl cysteine (Pam2Cys), an analog of Pam3Cys, has been synthesized (22) and been shown to correspond to the lipid moiety of macrophage-activating lipopeptide 2 isolated from myoplasma that lack cell walls (23)(24)(25). In contrast to Pam3Cys, Pam2Cys has only two ester-bound palmitic acids and a free amino group, which leads to improved water solubility of Pam2Cys-peptide constructs compared with Pam3Cys-peptide constructs.…”

Section: Highly Immunogenic and Totally Synthetic Lipopeptides Asmentioning

confidence: 99%

Highly Immunogenic and Totally Synthetic Lipopeptides as Self-Adjuvanting Immunocontraceptive Vaccines

Zeng

Ghosh

Lau

et al. 2002

The Journal of Immunology

179

188

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In this study, we describe the synthesis of various lipopeptides based on the sequence of luteinizing hormone-releasing hormone (LHRH) and report on their abilities to induce Abs against this “self” hormone when inoculated into mice in the absence of additional adjuvant. The peptides consisted of a colinear CD4+ T helper cell epitope from the L chain of influenza virus hemagglutinin and LHRH, which has B cell epitopes but no T cell epitopes present in its sequence. Lipids were attached either at the N terminus or between the T cell epitope and LHRH, in the approximate center of the peptide. The lipopeptide constructs displayed different solubilities and immunological properties that depended not only on the lipid content but also on the position of attachment of the lipids. Some of these constructs were highly immunogenic, inducing high titers of Ab, which were capable of efficiently sterilizing female mice when administered in saline by s.c. or intranasal routes. The most effective vaccines were highly soluble, contained the dipalmitoyl-S-glyceryl cysteine moiety, and had this lipid attached at the center of the molecule. The relative ability of the lipopeptides to induce an Ab response in the absence of external adjuvant was reflected by their ability to up-regulate the surface expression of MHC class II molecules on immature dendritic cells. These results demonstrate that the composition and position within peptide vaccines of self-adjuvanting lipid groups can influence the ability to induce the maturation of dendritic cells and, in turn, the magnitude of the resulting Ab response.

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Activation of nuclear factor-κB in macrophages by mycoplasmal lipopeptides

Cited by 37 publications

References 31 publications

Mycoplasma fermentans inhibits tumor necrosis factor α-induced apoptosis in the human myelomonocytic U937 cell line

Mycoplasma fermentans inhibits tumor necrosis factor α-induced apoptosis in the human myelomonocytic U937 cell line

Mycoplasma arginini enhances cytotoxicity of thioglycollate-elicited murine macrophages toward YAC-1 tumor cells through production of NO

Highly Immunogenic and Totally Synthetic Lipopeptides as Self-Adjuvanting Immunocontraceptive Vaccines

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