43 research outputs found
Lack of Galectin-3 Drives Response to Paracoccidioides brasiliensis toward a Th2-Biased Immunity
There is recent evidence that galectin-3 participates in immunity to infections, mostly by tuning cytokine production. We studied the balance of Th1/Th2 responses to P. brasiliensis experimental infection in the absence of galectin-3. The intermediate resistance to the fungal infection presented by C57BL/6 mice, associated with the development of a mixed type of immunity, was replaced with susceptibility to infection and a Th2-polarized immune response, in galectin-3-deficient (gal3−/−) mice. Such a response was associated with defective inflammatory and delayed type hypersensitivity (DTH) reactions, high IL-4 and GATA-3 expression and low nitric oxide production in the organs of infected animals. Gal3−/− macrophages exhibited higher TLR2 transcript levels and IL-10 production compared to wild-type macrophages after stimulation with P. brasiliensis antigens. We hypothesize that, during an in vivo P. brasiliensis infection, galectin-3 exerts its tuning role on immunity by interfering with the generation of regulatory macrophages, thus hindering the consequent Th2-polarized type of response
Immunohistochemical demonstration of TGF-ß and decorin in paracoccidioidal granulomas
Avaliação do cetoconazol em camundongos inoculados com Paracoccidioides brasiliensis pela histopatologia de fÃgado e baço e pela intradermorreação de paracoccidioidina
Phospholipase gene expression during Paracoccidioides brasiliensis morphological transition and infection
Kinetics of IFN-gamma, TNF-alpha, IL-10 and IL-4 production by mononuclear cells stimulated with gp43 peptides, in patients cured of paracoccidioidomycosis
Gelatinase activity of exoantigens from virulent and non-virulent isolates of Paracoccidioides brasiliensis
Differences in the occurrence of components with gelatinase activity were detected among four isolates of Paracoccidioides brasiliensis: Pb339 and Pb18 (highly virulent), and Pb265 and Pb18AV (very low virulence). Culture filtrates from these isolates were electrophoresed in substrate gels and tested for gelatinase activity. Pb339 showed three enzyme bands of apparent molecular masses: 43, 53 and 78 kDa; Pb18 had two bands, one at 59 kDa and another with molecular mass higher than 78 kDa. Isolate Pb18AV showed only one band at 78 kDa and Pb265 exhibited a component of molecular mass which failed to enter the separating gel.CENT PUBL HLTH LAB,MYCOL REFERENCE LAB,LONDON,ENGLANDESCOLA PAULISTA MED,DEPT MOLEC BIOL,SAO PAULO,SP,BRAZILESCOLA PAULISTA MED,DEPT MOLEC BIOL,SAO PAULO,SP,BRAZILWeb of Scienc