What's new for 'Trypanosomatids' in PubMed

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Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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PubMed Results

Items 1 -10 of 21

198862632009110420091209

1505-17731232009Pol J Vet SciAccidental discovery of Trypanosoma theileri in the in vitro culture of the heifer lymphocytes.395-8The diagnostics of the Trypanosoma sp. invasion by means of the classic methods i.e. the methods of thin smears or thick drop or even the microhematocrite method, especially when intensity of infection is low, is very difficult. In our climatic zone, trypanosomosis is usually considered as an exotic disease. An opportunistic model of the infection with the parasite and a lack of current data on the prevalence of T. theileri in the cattle in Poland cause that it is neglected as a potential reason of contamination of tissue cultures in cattle. We showed the presence of T. theileri in culture of isolated lymphocytes from one of six heifers examined. It seems that the prevalence of the invasion of the parasite is not very intense but it should be considered as a possible threat for bovine cell culture. It is also worth including this parasitosis in the differential diagnostics of other diseases that are infectious and/or proceed with symptoms of immunosuppression.Parasitology Unit, Department of Internal and Parasitic Diseases with Clinic of Horses, Dogs and Cats Diseases, Wrocław University of Environmental and Life Sciences, C.K. Norwida 31, 50-375 Wrocław. zenon.soltysiak@up.wroc.plSołtysiakZZGorczykowskiMMPawlas-OpielaMMChełmońska-SoytaAANowackiWWengJournal Article

PolandPol J Vet Sci1011254731505-1773IMAnimalsCattleCell Culture TechniquesveterinaryFemaleLymphocytescytologyparasitologyTrypanosomaisolation & purification2009115602009115602009121660ppublish19886263198807412009112020091215

1091 -6490106462009Nov17Proc. Natl. Acad. Sci. U.S.A.A mechanism for functional segregation of mitochondrial and cytosolic genetic codes.19420-5The coexistence of multiple gene translation machineries is a feature of eukaryotic cells and a result of the endosymbiotic events that gave rise to mitochondria, plastids, and other organelles. The conditions required for the integration of these apparatuses within a single cell are not understood, but current evidence indicates that complete ablation of the mitochondrial protein synthesis apparatus and its substitution by its cytosolic equivalent is not possible. Why certain mitochondrial components and not others can be substituted by cytosolic equivalents is not known. In trypanosomatids this situation reaches a limit, because certain aminoacyl-tRNA synthetases are mitochondrial specific despite the fact that all tRNAs in these organisms are shared between cytosol and mitochondria. Here we report that a mitochondria-specific lysyl-tRNA synthetase in Trypanosoma has evolved a mechanism to block the activity of the enzyme during its synthesis and translocation. Only when the enzyme reaches the mitochondria is it activated through the cleavage of a C-terminal structural extension, preventing the possibility of the enzyme being active in the cytosol.Institute for Research in Biomedicine, Barcelona, Catalonia, Spain.EspañolYaizaYThutDanielDSchneiderAndréAde PouplanaLluís RibasLRengJournal ArticleResearch Support, Non-U.S. Gov't20091030

United StatesProc Natl Acad Sci U S A75058760027-8424EC 6.1.1.6Lysine-tRNA LigaseIMAmino Acid SequenceCytosolenzymologyLysine-tRNA LigasebiosynthesisgeneticsmetabolismMitochondriaenzymologygeneticsMolecular Sequence DataProtein BiosynthesisProtein TransportSequence Analysis, ProteinTransfer RNA AminoacylationTrypanosoma brucei bruceienzymologygeneticsPMC2780774 [Available on 05/17/10]2009103020091136020091136020091216602010517ppublish090993710610.1073/pnas.090993710619880741PMC2780774198572632009110520091201

1471-2164102009BMC GenomicsTranscriptome analysis of differentiating trypanosomes reveals the existence of multiple post-transcriptional regulons.495BACKGROUND: Trypanosome gene expression is regulated almost exclusively at the post-transcriptional level, with mRNA degradation playing a decisive role. When trypanosomes are transferred from the blood of a mammal to the midgut of a Tsetse fly, they transform to procyclic forms: gene expression is reprogrammed, changing the cell surface and switching the mode of energy metabolism. Within the blood, trypanosomes can pre-adapt for Tsetse transmission, becoming growth-arrested stumpy forms. We describe here the transitions in gene expression that occur during differentiation of in-vitro cultured bloodstream forms to procyclic forms. RESULTS: Some mRNAs showed changes within 30 min of cis-aconitate addition, whereas others responded 12-24 hours later. For the first 12 h after addition of cis-aconitate, cells accumulated at the G1 phase of the cell cycle, and showed decreases in mRNAs required for proliferation, mimicking the changes seen in stumpy forms: many mRNAs needed for ribosomal and flagellar biogenesis showed striking co-regulation. Other mRNAs encoding components of signal transduction pathways and potential regulators were specifically induced only during differentiation. Messenger RNAs encoding proteins required for individual metabolic pathways were often co-regulated. CONCLUSION: Trypanosome genes form post-transcriptional regulons in which mRNAs with functions in particular pathways, or encoding components of protein complexes, show almost identical patterns of regulation.Zentrum für Molekulare Biologie der Universität Heidelberg, ZMBH-DKFZ Alliance, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany. r.queiroz@dkfz-heidelberg.deQueirozRafaelRBenzCorinnaCFellenbergKurtKHoheiselJörg DJDClaytonChristineCengJournal ArticleResearch Support, Non-U.S. Gov't20091026

EnglandBMC Genomics1009652581471-21640RNA, Messenger0RNA, ProtozoanIMCluster AnalysisGene Expression ProfilingGene Expression Regulation, DevelopmentalOligonucleotide Array Sequence AnalysisRNA Processing, Post-TranscriptionalRNA, MessengermetabolismRNA, ProtozoanmetabolismRegulonTrypanosomageneticsgrowth & developmentmetabolismPMC277286420094212009102620091026200910286020091028602009121660epublish1471-216 4-10-49510.1186/1471-2164-10-49519857263PMC2772864198061542009101620091123

1740-15347112009NovNat. Rev. Microbiol.The trypanosome flagellar pocket.775-86Trypanosomes are important disease agents and excellent models for the study of evolutionary cell biology. The trypanosome flagellar pocket is a small invagination of the plasma membrane where the flagellum exits the cytoplasm and participates in many cellular processes. It is the only site of exocytosis and endocytosis and part of a multiorganelle complex that is involved in cell polarity and cell division. Several flagellar pocket-associated proteins have been identified and found to contribute to trafficking and virulence. In this Review we discuss the contribution of the flagellar pocket to protein trafficking, immune evasion and other processes.Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, UK. mcf34@cam.ac.ukFieldMark CMCCarringtonMarkMengWellcome TrustUnited KingdomJournal ArticleResearch Support, Non-U.S. Gov'tReview20091006

EnglandNat Rev Microbiol1011902611740-15260Protozoan ProteinsIMAnimalsCattleCell MembranemetabolismultrastructureFlagellametabolismultrastructureHumansLife Cycle StagesProtein TransportProtozoan ProteinsgeneticsmetabolismTrypanosoma brucei bruceimetabolismphysiologyultrastructureTrypanosomiasis, Africanimmunologymetabolismparasitology114200910062009107602009107602009121660ppublishnrmicro222110.1038/nrmicro222119806154197737652009092320091215

0093-735538102009OctLab Anim (NY)Cunning parasite manipulates immune system.312DoransKirstenKengNews

United StatesLab Anim (NY)04177370093-7355EC 3.5.3.1ArginaseIMAnimalsArginasemetabolismDisease Models, AnimalDisease VectorsFemaleHost-Parasite InteractionsimmunologyLeishmaniaimmunologypathogenicityLeishmaniasis, CutaneousimmunologytransmissionMacrophagesenzymologyimmunologyMicePsychodidaeparasitology2009924602009924602009121660ppublishlaban1009-312b10.1038/laban1009-312b19773765197693572009101520091124

1520-480452202009Oct22J. Med. Chem.Structure-guided development of selective TbcatB inhibitors .6489-93The trypanosomal cathepsin TbcatB is essential for parasite survival and is an attractive therapeutic target. Herein we report the structure-guided development of TbcatB inhibitors with specificity relative to rhodesain and human cathepsins B and L. Inhibitors were tested for enzymatic activity, trypanocidal activity, and general cytotoxicity. These data chemically validate TbcatB as a drug target and demonstrate that it is possible to potently and selectively inhibit TbcatB relative to trypanosomal and human homologues.Graduate Program in Chemistry and Chemical Biology, University of California, San Francisco, California 94143-2280, USA.MallariJeremy PJPShelatAnang AAAKosinskiAaronACaffreyConor RCRConnellyMicheleMZhuFangyiFMcKerrowJames HJHGuyR KiplinRKengAI35707AINIAID NIH HHSUnited StatesJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov't

United StatesJ Med Chem97165310022-26230Protease Inhibitors0Purines0Trypanocidal AgentsEC 3.4.22.-Cysteine EndopeptidasesEC 3.4.22.-TbcatB protein, Trypanosoma bruceiEC 3.4.22.-rhodesainEC 3.4.22.1Cathepsin BEC 3.4.22.15Cathepsin LIMAnimalsCathepsin Bantagonists & inhibitorsmetabolismCathepsin Lantagonists & inhibitorsmetabolismCell LineCysteine EndopeptidaseschemistrymetabolismDrug DiscoveryHumansModels, MolecularProtease InhibitorschemistrypharmacologyProtein ConformationPurineschemistrySubstrate SpecificityTrypanocidal AgentschemistrypharmacologyTrypanosoma brucei bruceidrug effectsenzymolo gyNIHMS143455 [Available on 10/22/10]PMC2762491 [Available on 10/22/10]200992360200992360200912166020101022ppublish10.1021/jm900908p19769357PMC2762491NIHMS143455197483172009092120091209

1471-500725102009OctTrends Parasitol.Surprising variety in energy metabolism within Trypanosomatidae.482-90The metabolism of Trypanosomatidae differs significantly between distinct species and can even be completely different between various life-cycle stages of the same species. It has been proposed that differences in energy metabolism are related to differences in nutrient supply in the environments of the various trypanosomatids. However, the literature shows that availability of substrates does not dictate the type of energy metabolism of trypanosomatids, as Trypanosoma theileri, Trypanosoma lewisi and African trypanosomes all live in the bloodstream of their mammalian host, but have surprisingly large differences in metabolism. Furthermore, in trypanosomatids no obvious relationship exists between energy metabolism and phylogeny or mode of transmission. We provide an overview of the metabolic capacities in the energy metabolism of distinct trypanosomatids, and suggest that these can be divided into four different metabolic categories of increasing complexity.Department of Medical Microbiology and Infectious Diseases, Erasmus MC, University Medical Centre Rotterdam, 'S Gravendijkwal 230, 3015 CE Rotterdam, The Netherlands. a.tielens@erasmusmc.nlTielensAloysius G MAGvan HellemondJaap JJJengJournal ArticleReview20090910

EnglandTrends Parasitol1009660341471-4922IMAnimalsBloodparasitologyEnergy MetabolismHost-Parasite InteractionsLife Cycle StagesSpecies SpecificityTrypanosomatinaclassificationgrowth & developmentmetabolismphysiology53200926200972200971420099102009915602009915602009121660ppublishS1471-4922(09)00165-210.1016/j.pt.2009.07.00719748317197241372009090220091207

1744-309165Pt 92009Sep1Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.Crystallization and preliminary X-ray analysis of aspartate transcarbamoylase from the parasitic protist Trypanosoma cruzi.933-6Aspartate transcarbamoylase (ATCase), the second enzyme of the de novo pyrimidine-biosynthetic pathway, catalyzes the production of carbamoyl aspartate from carbamoyl phosphate and L-aspartate. In contrast to Escherichia coli ATCase and eukaryotic CAD multifunctional fusion enzymes, Trypanosoma cruzi ATCase lacks regulatory subunits and is not part of the multifunctional fusion enzyme. Recombinant T. cruzi ATCase expressed in E. coli was purified and crystallized in a ligand-free form and in a complex with carbamoyl phosphate at 277 K by the sitting-drop vapour-diffusion technique using polyethylene glycol 3350 as a precipitant. Ligand-free crystals (space group P1, unit-cell parameters a = 78.42, b = 79.28, c = 92.02 A, alpha = 69.56, beta = 82.90, gamma = 63.25 degrees) diffracted X-rays to 2.8 A resolution, while those cocrystallized with carbamoyl phosphate (space group P2(1), unit-cell parameters a = 88.41, b = 158.38, c = 89.00 A, beta = 119.66 degrees) diffracted to 1.6 A resolution. The presence of two homotrimers in the asymmetric unit (38 kDa x 6) gives V(M) values of 2.3 and 2.5 A(3) Da(-1) for the P1 and P2(1) crystal forms, respectively.Department of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Kyoto, Japan.MatobaKazuakiKNaraTakeshiTAokiTakashiTHonmaTerukiTTanakaAkikoAInoueMasayukiMMatsuokaShigeruSInaokaDaniel KenDKKitaKiyoshiKHaradaShigeharuSengJournal ArticleResearch Support, Non-U.S. Gov't20090826

EnglandActa Crystallogr Sect F Struct Biol Cryst Commun101226117EC 2.1.3.2Aspartate CarbamoyltransferaseIMAnimalsAspartate CarbamoyltransferasechemistryCrystallizationCrystallography, X-RayElectrophoresis, Polyacrylamide GelParasitesenzymologyStatic ElectricityTrypanosoma cruzienzymology2009423200981220098262009939020099 3602009121660ppublishS174430910903195910.1107/S174430910903195919724137197127682009100920091130

1873-251827442009Oct19J. Inorg. Biochem.A novel vanadyl complex with a polypyridyl DNA intercalator as ligand: a potential anti-protozoa and anti-tumor agent.1386-94In the search for new metal-based drugs for the treatment of tumoral and parasitic diseases a vanadyl complex, [V(IV)O(SO(4))(H2O)(2)(dppz)].2H(2)O, that includes the bidentate polypyridyl DNA intercalator dipyrido[3,2-a:2',3'-c]phenazine (dppz), was synthesized, characterized by a combination of techniques, and in vitro evaluated on the human acute promyelocytic leukemia cell line HL-60 and against Dm28c strain epimastigotes of the parasite Trypanosoma cruzi, causative agent of Chagas' disease. EPR spectroscopy suggests a distorted octahedral geometry for the complex with the dppz ligand acting as bidentate, binding through both nitrogen donor atoms in an axial-equatorial mode. An oxo group, two water molecules and a sulphate donor occupy the remainder coordination positions. The complex, as well as the anti-trypanosomal reference drug Nifurtimox, showed IC(50) values in the muM range against T. cruzi Dm28c strain. In addition the complex exhibited excellent in vitro anti-tumor activity against leukemia (HL-60 cell line) comparable to that of cisplatin, inducing cell death by apoptosis with IC(50) values in the micromolar range. Data from gel electrophoresis and atomic force microscopy indicate that the complex interacts with DNA, suggesting that its mechanism of action may include DNA as a target. EPR and (51)V NMR experiments were also carried out with aged aerated solutions of the complex to get insight into the stability of the complex in solution and the species responsible for the in vitro activities observed.Cátedra de Química Inorgánica, Facultad de Química, Universidad de la República, Gral. Flores 2124, C. C. 1157, 11800 Montevideo, Uruguay.BenítezJulioJGuggeriLucíaLTomazIsabelIPessoaJoão CostaJCMorenoVirtudesVLorenzoJuliaJAvilésFrancesc XFXGaratBeatrizBGambinoDinorah DengJournal ArticleResearch Support, Non-U.S. Gov't20090724

United StatesJ Inorg Biochem79057880162-01340Antineoplastic Agents0Antiprotozoal Agents0Intercalating Agents0Phenazines0Vanadates0dipyrido(3,2-a-2',3'-c)phenazineIMAnimalsAntineoplastic Agentschemical synthesischemistrypharmacologyAntiprotozoal Agentschemical synthesischemistrypharmacologyApoptosisdrug effectsChagas Diseasedrug therapyDose-Response Relationship, DrugDrug Screening Assays, AntitumorHL-60 CellsHumansIntercalating Agentschemical synthesischemistrypharmacologyNeoplasmsdrug therapyPhenazineschemical synthesischemistrypharmacologyTrypanosoma cruzigrowth & developmentVanadateschemical synthesischemistrypharmacology2009521200971200971520097242009822902009822902009121660ppublishS0162-0134(09)00159-710.1016/j.jinorgbio.2009.07.01319695708