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H Saklani-Jusforgues

Publications and source records attributed to H Saklani-Jusforgues.

8 recordsLinked to original sources
PubMed2001

Early translocation of acid-adapted Listeria monocytogenes during enteric infection in TNF/LTalpha-/- mice.

TNF/LTalpha deficient mice are devoid of Peyer's patches and lack mesenteric lymph nodes. Translocation, especially in the early steps after intragastric delivery of Listeria monocytogenes, has been explored in this study, and the role of TNFalpha has been addressed. We showed that L. monocytogenes translocation occurred at least as efficiently in TNF/LTalpha-/- mice as in TNF/LTalpha+/+ littermates. Even very low inocula (2.7x10(4) cfu) could initiate infection in the TNF/LTalpha deficient mice. Early kinetics of dissemination to the spleen and liver were similar, L. monocytogenes reaching these organs at 8 h post inoculation. However, a 10-fold higher bacterial load was observed at this early time point in the TNF/LTalpha deficient mice. rTNF pretreatment (4 h before intragastric inoculation) had no effect on the L. monocytogenes associated with the caecum-colon walls at 10 h after inoculation, although bacterial levels in the caecum-colon lumen and in spleen and liver were already controlled.

Animals↗
PubMed2001

Characterisation of a Listeria monocytogenes mutant deficient in D-arabitol fermentation.

We selected and analysed a Tn917-lac Listeria monocytogenes mutant deficient in D-arabitol fermentation. Comparison of the 310-aa-long translated partial sequence of the disrupted gene with known proteins showed similarity with the phosphotransferase system galactitol-specific enzyme IIC component of the alkaliphilic Bacillus halodurans (50% identity) and of Escherichia coli (36% identity). Fermentation of 18 other carbohydrates was unimpaired, suggesting the specificity of this transmembrane permease IIC for the pentitol D-arabitol. The deficiency in D-arabitol fermentation did not alter L. monocytogenes virulence in the BALB/c mouse model after intravenous and intragastric inoculations. This fully virulent mutant is a valuable tool to study L. monocytogenes oral infection, since the antibiotic resistance marker present on the Tn917-lac transposon will efficiently select L. monocytogenes against the intestinal microflora.

Animals↗
PubMed2000

Effect of acid-adaptation on Listeria monocytogenes survival and translocation in a murine intragastric infection model.

Acid tolerance response mechanisms can greatly influence Listeria monocytogenes survival in low pH foods. In the present paper, the effect of acid-adaptation together with control of gastric pH level on L. monocytogenes survival and translocation was analyzed after intragastric inoculation in the BALB/c mouse model. Our results showed that acid-adaptation led to an increase in resistance to the first barrier constituted by the low gastric pH and that inoculation at alkaline pH had a synergistic effect. It resulted in a higher live bacterial load reaching the next intestinal compartments and was correlated with increased translocation rates to the mesenteric lymph nodes, both at the frequency and quantitative levels. Our results in this murine model suggest that acid-adaptation of L. monocytogenes in low pH foods, together with control of gastric pH level through dietary practices, or use of inhibitors of gastric acid secretion, may be potential aggravating risk factors to food-borne listeriosis.

Adaptation, Physiological↗
PubMed1997

The anti-tumoral activity of human glycoprotein HGP.92: a study with the mouse Lewis-lung-tumor cell.

The ability of a purified human glycoprotein (HGP.92) to exert anti-tumor activity was investigated in a mouse model using long-term readout assays. In vitro, in the presence of inflammatory mouse macrophages incubated with HGP.92, the growth of the mouse Lewis-lung-tumor cells (3LL) was decreased. This effect was concentration-dependent and required direct contact between tumor targets and HGP.92-treated macrophages. In addition, if the macrophage monolayer was depleted of HGP.92 before addition of the target cells, no more cytostatic effect was observed. This anti-tumor activity of HGP.92-treated mouse macrophage was partially abrogated by addition of catalase in the culture medium, but not by superoxide dismutase or scavengers of the hydroxyl radical and singlet oxygen. Moreover, this tumor-cell growth reduction was not dependent on nitric oxide. In vivo, multiple i.v. injections of HGP.92 (5 times, 3 days apart) during the first week and a half exerted significant anti-tumor activity, as assessed by the reduction of both the number and the size of the lung nodules 3 weeks after i.v. inoculation of 3LL cells.

Adjuvants, Immunologic↗
PubMed1995

Human glycoprotein HGP92 induces cytokine synthesis in mouse mononuclear phagocytes.

HGP92 has been shown to enhance in vitro and in vivo the bactericidal and tumoricidal activity of mouse macrophages. In this study we investigated the effect of HGP92 on the accumulation of cytokine mRNA in mouse inflammatory, peritoneal macrophages and the monocytic cell line J774. HGP92 significantly enhanced the level of cytokine mRNA for IL-1 alpha, IL-1 beta, IL-6, IL-10, IL-12, TNF-alpha and GM-CSF during the first 24 h of the incubation. This effect triggered by HGP92 was comparable to that obtained with lipopolysaccharide (LPS), which is a strong cytokine inducer. This accumulation of cytokine mRNA in macrophages was correlated with secretion of IL-6 and TNF-alpha in cell supernatant. The release of IL-6 was HGP92 concentration dependent over a range of 0.3-10 micrograms/ml with a maximum production obtained after a 24 h incubation of inflammatory macrophages with HGP92. This effect was shown not to be due to contamination of HGP92 by LPS since inflammatory macrophages from C57BL/6 mice were responsive to HGP92 pretreated with polymyxin B sulfate and unresponsive to heated HGP92. Stimulating activity of HGP92 was confirmed using macrophages from C3H/HeJ mice. These results suggest that HGP92 might modulate the immune responses by increasing cytokine production by macrophages.

Adjuvants, Immunologic↗
PubMed1994

A 92-kDa human immunostimulatory protein.

We purified to apparent homogeneity a human urinary glycoprotein of 92 kDa (HGP.92) that, administered intravenously at 250 micrograms/kg, fully protected mice against a lethal inoculum of Listeria monocytogenes. Since HGP.92 protected scid mice, which lack B and T lymphocytes, this increased resistance to Listeria did not appear to be lymphocyte mediated. Furthermore, inflammatory macrophages incubated with 6 nM HGP.92 inhibited the growth of Lewis carcinoma cells in vitro. These two activities appeared to depend on an oligosaccharide moiety, as they were lost after N-Glycanase treatment of HGP.92. Thus, the biological activity of HGP.92 was in some way related to a glycan moiety.

Amino Acid Sequence↗
PubMed1992

Immunostimulatory human urinary protein.

We have previously extracted a protein from inflammatory mouse granuloma that fully protects normal mice against lethal Listeria monocytogenes infection. We now report that polyclonal antibodies directed against this protein react with a human urinary fraction that also provides full protection of normal mice against L. monocytogenes. Murine monoclonal antibodies completely inhibit the protective activity of the human urinary fraction. We have purified to apparent homogeneity a human glycoprotein of 43 kDa (HGP.43), pI = 3.2 +/- 0.2. HGP.43 injected i.v. at 250 micrograms/kg fully protected mice against a lethal inoculum of L. monocytogenes. Such resistance followed injection of HGP.43, 4 days before and, still significantly, 8 hr after Listeria infection. In scid mice lacking T and B cells, similar resistance to L. monocytogenes was observed. Inflammatory murine macrophages became cytostatic against Lewis carcinoma cells after incubation with 1.5 nM HGP-43.

Animals↗