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Sent on Wednesday, 2012 May 30Search: kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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| PubMed Results |
| 1. | Rev Bras Reumatol. 2012 Jun;52(3):450-452.Cutaneous leishmaniasis in a patient with ankylosing spondylitis using adalimumab. [Article in English, Portuguese] Gomes KW, Benevides AN, Vieira FJ, Burlamaqui MP, Vieira MD, Fontenelle LM.SourceHospital Geral de Fortaleza. AbstractLeishmaniasis is an anthropozoonosis caused by species of Leishmania and can have different clinical presentations, depending on the parasite-host relationship. Tumor necrosis factor-α (TNF-α) is a cytokine essential to infection control, especially against intracellular parasites such as Leishmania. Anti-TNF-α strategies have had a marked impact on the treatment of rheumatic diseases, but the clinical use of those antagonists has been accompanied by an increased report of infections. We report the first case of cutaneous leishmaniasis in a patient with ankylosing spondylitis treated with adalimumab and methotrexate in Brazil. We believe that, in this case, there was no association between the anti-TNF-α treatment and cutaneous leishmaniasis, because the disease was limited to only one ulcer that healed completely after treatment. More studies, however, are necessary to better understand the possible relationship between anti-TNF-α agents and leishmaniasis. |
| PMID: 22641598 [PubMed - as supplied by publisher] | |
| 2. | J Control Release. 2012 May 25. [Epub ahead of print]PLGA nanoparticles and nanosuspensions with amphotericin B: Potent in vitro and in vivo alternatives to Fungizone® and AmBisome®Van de Ven H, Paulussen C, Feijens PB, Matheeussen A, Rombaut P, Kayaert P, Van den Mooter G, Weyenberg W, Cos P, Maes L, Ludwig A.SourceLaboratory of Pharmaceutical Technology and Biopharmacy, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp (Wilrijk), Belgium. AbstractThis paper describes the development of poly(D,L-lactide-co-glycolide) (PLGA) nanoparticles (NPs) and nanosuspensions with the polyene antibiotic amphotericin B (AmB). The nanoformulations were prepared using nanoprecipitation and were characterised with respect to size, zeta potential, morphology, drug crystallinity and content. Standard in vitro sensitivity tests were performed on MRC-5 cells, red blood cells, Leishmania infantum promastigotes and intracellular amastigotes and the fungal species Candida albicans, Aspergillus fumigatus and Trichophyton rubrum. The in vivo efficacy was assessed and compared to that of Fungizone® and AmBisome® in the acute A. fumigatus mouse model at a dose of 2.5 and 5.0mg/kg AmB equivalents. The developed AmB nanoformulations were equivalently or more effective against the different Leishmania stages and axenic fungi in comparison with the free drug. The in vitro biological activity, and especially hemolytic activity, clearly depended on the preparation parameters of the different nanoformulations. Further, we demonstrated that the superior in vitro antifungal activity could be extrapolated to the in vivo situation. At equivalent dose, the optimal AmB-loaded PLGA NP was about two times and the AmB nanosuspension about four times more efficacious in reducing the total burden than AmBisome®. The developed AmB nanomedicines could represent potent and cost-effective alternatives to Fungizone® and AmBisome®. Copyright © 2012. Published by Elsevier B.V. |
| PMID: 22641062 [PubMed - as supplied by publisher] | |
| 3. | FEBS Lett. 2012 May 25. [Epub ahead of print]Trypanosomes contain two highly different isoforms of peroxin PEX13 involved in glycosome biogenesis.Brennand A, Rigden DJ, Michels PA.SourceResearch Unit for Tropical Diseases, de Duve Institute and Laboratory of Biochemistry, Université catholique de Louvain, Avenue Hippocrate 74, postal box B1.74.01, B-1200 Brussels, Belgium. AbstractWe previously identified the peroxin PEX13 in Trypanosoma brucei. Although lacking some features considered typical of PEX13s, it appeared functional in the biogenesis of glycosomes, the peroxisome-like organelles of trypanosomatids. Here we report the identification of a very different trypanosomatid PEX13, not containing the commonly encountered PEX13 SH3 domain but having other typical features. It is readily detected with the jackhmmer database search program, but not with PSI-BLAST. This is the first time different PEX13 isoforms are reported in a single organism. We show that this PEX13.2, like the PEX13.1 previously described, is associated with glycosomes and that its depletion by RNA interference affects the biogenesis of the organelles and viability of trypanosomes. The features considered typical of PEX13s are discussed. Copyright © 2012. Published by Elsevier B.V. |
| PMID: 22641036 [PubMed - as supplied by publisher] | |
| 4. | Gene. 2012 May 1;498(2):147-54. Epub 2012 Feb 25.Cloning, localization and differential expression of the Trypanosoma cruzi TcOGNT-2 glycosyl transferase.Chiribao ML, Libisch MG, Osinaga E, Parodi-Talice A, Robello C.SourceUnidad de Biología Molecular, Institut Pasteur de Montevideo, Uruguay. AbstractThe surface of Trypanosoma cruzi is covered by a dense glycocalix which is characteristic of each stage of the life cycle. Its composition and complexity depend mainly on mucin-like proteins. A remarkable feature of O-glycan biosynthesis in trypanosomes is that it initiates with the addition of a GlcNAc instead of the GalNAc residue that is commonly used in vertebrate mucins. The fact that the interplay between trans-sialidase and mucin is crucial for pathogenesis, and both families have stage-specific members is also remarkable. Recently the enzyme that transfers the first GlcNAc from UDP-GlcNAc to a serine or threonine residue was kinetically characterized. The relevance of this enzyme is evidenced by its role as catalyzer of the first step in O-glycosylation. In this paper we describe how this gene is expressed differentially along the life cycle with a pattern that is very similar to that of trans-sialidases. Its localization was determined, showing that the protein predicted to be in the Golgi apparatus is also present in reservosomes. Finally our results indicate that this enzyme, when overexpressed, enhances T. cruzi infectivity. Copyright © 2012 Elsevier B.V. All rights reserved. |
| PMID: 22387207 [PubMed - indexed for MEDLINE] | |
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| 5. | Int J Biol Sci. 2011;7(9):1357-70. Epub 2011 Nov 1.Gastrointestinal infection with Mexican TcI Trypanosoma cruzi strains: different degrees of colonization and diverse immune responses.Espinoza B, Solorzano-Domínguez N, Vizcaino-Castillo A, Martínez I, Elias-López AL, Rodríguez-Martínez JA.SourceDepartamento de Inmunología. Instituto de Investigaciones Biomédicas. Universidad Nacional Autónoma de México, Mexico City 04510. besgu@biomedicas.unam.mx AbstractMexican Ninoa and Queretaro (Qro) TcI strains of Trypanosoma cruzi have shown different degrees of virulence, and the two strains produce heterogeneous immune responses in the hearts of infected mice. This work shows that the same strains can invade the intestine by an intraperitoneal route and establish an infection, mainly in the colon. The three segments of the small intestine (duodenum, jejunum and ileum) were infected to a lesser degree than the colon. Despite the fact that parasites were predominantly found in the colon, an obvious inflammatory reaction was observed in the submucosal layer along the entire intestinal tract, with the virulent Qro strain causing significantly more areas of higher immune infiltration. A clear recruitment of CD4⁺ and CD8⁺ T lymphocytes to the mesenteric ganglia was observed during infection with the virulent strain. Macrophages were also differentially distributed in the gastrointestinal tract. These later cells infiltrated fewer amastigote nests in the mice infected with the Qro strain than in the mice infected with the Ninoa strain. When IFN-γ, TNF-α, and IL-4 levels were measured, an increase in these cytokines was observed compared with the uninfected mice. The role of these inflammatory reactions in the pathogenesis of Chagas enteropathy is also discussed in this paper. |
| PMID: 22110387 [PubMed - indexed for MEDLINE] | |
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| 6. | Int J Biol Sci. 2011;7(9):1257-72. Epub 2011 Oct 25.The increase in mannose receptor recycling favors arginase induction and Trypanosoma cruzi survival in macrophages.Garrido VV, Dulgerian LR, Stempin CC, Cerbán FM.SourceCIBICI-CONICET, Dpto Bioquímica Clínica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina. AbstractThe macrophage mannose receptor (MR) is a pattern recognition receptor of the innate immune system that binds to microbial structures bearing mannose, fucose and N-acetylglucosamine on their surface. Trypanosoma cruzi antigen cruzipain (Cz) is found in the different developmental forms of the parasite. This glycoprotein has a highly mannosylated C-terminal domain that participates in the host-antigen contact. Our group previously demonstrated that Cz-macrophage (Mo) interaction could modulate the immune response against T. cruzi through the induction of a preferential metabolic pathway. In this work, we have studied in Mo the role of MR in arginase induction and in T. cruzi survival using different MR ligands. We have showed that pre-incubation of T. cruzi infected cells with mannose-Bovine Serum Albumin (Man-BSA, MR specific ligand) biased nitric oxide (NO)/urea balance towards urea production and increased intracellular amastigotes growth. The study of intracellular signals showed that pre-incubation with Man-BSA in T. cruzi J774 infected cells induced down-regulation of JNK and p44/p42 phosphorylation and increased of p38 MAPK phosphorylation. These results are coincident with previous data showing that Cz also modifies the MAPK phosphorylation profile induced by the parasite. In addition, we have showed by confocal microscopy that Cz and Man-BSA enhance MR recycling. Furthermore, we studied MR behavior during T. cruzi infection in vivo. MR was up-regulated in F4/80+ cells from T. cruzi infected mice at 13 and 15 days post infection. Besides, we investigated the effect of MR blocking antibody in T. cruzi infected peritoneal Mo. Arginase activity and parasite growth were decreased in infected cells pre-incubated with anti-MR antibody as compared with infected cells treated with control antibody. Therefore, we postulate that during T. cruzi infection, Cz may contact with MR, increasing MR recycling which leads to arginase activity up-regulation and intracellular parasite growth. |
| PMID: 22110379 [PubMed - indexed for MEDLINE] | |
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| 7. | Int J Biol Sci. 2011;7(9):1239-56. Epub 2011 Oct 25.Macrophage migration inhibitory factor (MIF): a key player in protozoan infections.Rosado Jde D, Rodriguez-Sosa M.SourceUnidad de Biomedicina, Facultad de Estudios Superiores Iztacala, Universidad Nacional Autónoma de México-UNAM, 54090 Tlalnepantla, Estado de México, México. AbstractMacrophage migration inhibitory factor (MIF) is a pleiotropic cytokine produced by the pituitary gland and multiple cell types, including macrophages (Mø), dendritic cells (DC) and T-cells. Upon releases MIF modulates the expression of several inflammatory molecules, such as TNF-α, nitric oxide and cyclooxygenase 2 (COX-2). These important MIF characteristics have prompted investigators to study its role in parasite infections. Several reports have demonstrated that MIF plays either a protective or deleterious role in the immune response to different pathogens. Here, we review the role of MIF in the host defense response to some important protozoan infections. |
| PMID: 22110378 [PubMed - indexed for MEDLINE] | |
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| 8. | Int J Biol Sci. 2011;7(9):1230-8. Epub 2011 Oct 25.A DNA vaccine encoding for TcSSP4 induces protection against acute and chronic infection in experimental Chagas disease.Arce-Fonseca M, Ramos-Ligonio A, López-Monteón A, Salgado-Jiménez B, Talamás-Rohana P, Rosales-Encina JL.SourceDepartamento de Infectómica y Patogenesis Molecular, Centro de Investigación y de Estudios Avanzados del I.P.N., México D.F. 07360, México. AbstractImmunization of mice with plasmids containing genes of Trypanosoma cruzi induces protective immunity in the murine model of Chagas disease. A cDNA clone that codes for an amastigote-specific surface protein (TcSSP4) was used as a candidate to develop a DNA vaccine. Mice were immunized with the recombinant protein rTcSSP4 and with cDNA for TcSSP4, and challenged with bloodstream trypomastigotes. Immunization with rTcSSP4 protein makes mice more susceptible to trypomastigote infection, with high mortality rates, whereas mice immunized with a eukaryotic expression plasmid containing the TcSSP4 cDNA were able to control the acute phase of infection. Heart tissue of gene-vaccinated animals did not show myocarditis and tissue damage at 365 days following infection, as compared with control animals. INF-γ was detected in sera of DNA vaccinated mice shortly after immunization, suggesting the development of a Th1 response. The TcSSP4 gene is a promising candidate for the development of an anti-T. cruzi DNA vaccine. |
| PMID: 22110377 [PubMed - indexed for MEDLINE] | |
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