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1.
FEMS Immunol Med Microbiol ; 66(1): 58-70, 2012 Oct.
Article in English | MEDLINE | ID: mdl-22574780

ABSTRACT

The macrophages are the first host cells that interact with the fungus Paracoccidioides brasiliensis, but the main mechanisms that regulate this interaction are not well understood. Because the role played by P. brasiliensis lipids in macrophage activation was not previously investigated, we aimed to assess the influence of diverse lipid fractions from P. brasiliensis yeasts in this process. The possible participation of TLR2 and TLR4 signaling was also evaluated using TLR2- and TLR4-defective macrophages. Four lipid-rich fractions were studied as follows: F1, composed by membrane phospholipids and neutral lipids, F2 by glycolipids of short chain, F3a by membrane glycoproteins anchored by glycosylphosphatidylinositol (GPI) groups, and F3b by glycolipids of long chain. All assayed lipid fractions were able to activate peritoneal macrophages and induce nitric oxide (NO) production. Importantly, the F1 and F3a fractions exerted opposite effects in the control of P. brasiliensis uptake and killing, but both fractions inhibited cytokines production. Furthermore, the increased NO production and expression of costimulatory molecules induced by F3a was shown to be TLR2 dependent although F1 used Toll-independent mechanisms. In conclusion, our work suggests that lipid components may play a role in the innate immunity against P. brasiliensis infection using Toll-dependent and independent mechanisms to control macrophage activation.


Subject(s)
Lipids/immunology , Macrophage Activation/drug effects , Macrophages, Peritoneal/immunology , Macrophages, Peritoneal/microbiology , Paracoccidioides/immunology , Animals , Cells, Cultured , Cytokines/metabolism , Lipids/isolation & purification , Mice , Mice, Inbred C3H , Mice, Inbred C57BL , Mice, Knockout , Microbial Viability , Nitric Oxide/metabolism , Paracoccidioides/chemistry , Toll-Like Receptor 2/immunology , Toll-Like Receptor 4/immunology
2.
Int J Parasitol ; 36(2): 165-73, 2006 Feb.
Article in English | MEDLINE | ID: mdl-16337632

ABSTRACT

Platelet-activating factor is a phospholipid mediator that exhibits a wide variety of physiological and pathophysiological effects, including induction of inflammatory response, chemotaxis and cellular differentiation. Trypanosoma cruzi, the etiological agent of Chagas' disease, is transmitted by triatomine insects and while in the triatomine midgut the parasite differentiates from a non-infective epimastigote stage into the pathogenic trypomastigote metacyclic form. We have previously demonstrated that platelet activating factor triggers in vitro cell differentiation of T. cruzi. Here we show a platelet activating factor-like activity isolated from lipid extract of T. cruzi epimastigotes incubated in the presence of [14C]acetate. Trypanosoma cruzi-platelet activating factor-like lipid induced the aggregation of rabbit platelets, which was prevented by platelet activating factor-acetylhydrolase. Mouse macrophage infection by T. cruzi was stimulated when epimastigotes were kept for 5 days in the presence of T. cruzi-platelet activating factor, before interacting with the macrophages. The differentiation of epimastigotes into metacyclic trypomastigotes was also triggered by T. cruzi-platelet activating factor. These effects were abrogated by a platelet activating factor antagonist, WEB 2086. Polyclonal antibody raised against mouse platelet activating factor receptor showed labelling for T. cruzi epimastigotes using immunoblotting and immunofluorescence assays. These data suggest that T. cruzi contain the components of an autocrine platelet activating factor-like ligand-receptor system that modulates cell differentiation towards the infectious stage.


Subject(s)
Macrophages/parasitology , Platelet Activating Factor/analysis , Protozoan Proteins/analysis , Trypanosoma cruzi/chemistry , Animals , Blotting, Western/methods , Fluorescent Antibody Technique , Life Cycle Stages , Mice , Platelet Activating Factor/pharmacology , Platelet Aggregation , Protozoan Proteins/pharmacology , Rabbits , Trypanosoma cruzi/growth & development
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