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Sent on Wednesday, 2009 Mar 04Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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| PubMed Results |
- 1: J Biol Chem. 2009 Mar 2. [Epub ahead of print]
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A type III protein arginine methyltransferase from the protozoan parasite, trypanosoma brucei.
Microbiology and Immunology, University at Buffalo, Buffalo, NY 14214.
Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). The ancient protozoan parasite, Trypanosoma brucei, possesses five putative PRMTs, a relatively large number for a single-celled eukaryote. Trypanosomatids lack gene regulation at the level of transcription, instead relying on posttranscriptional control mechanisms that act at the levels of RNA turnover, translation, and editing, all processes that likely involve multiple RNA binding proteins, which are common targets of arginine methylation. Here, we report the characterization of a trypanosome PRMT, TbPRMT7, which is homologous to human PRMT7. Interestingly, trypanosomatids are the only single-celled eukaryotes known to harbor a PRMT7 homologue. TbPRMT7 differs dramatically from all known metazoan PRMT7 homologues in lacking the second AdoMet binding-like domain that is required for activity of the human enzyme. Nevertheless, bacterially expressed TbPRMT7 exhibits robust methyltransferase activity towards multiple targets in vitro. High resolution ion exchange chromatography analysis of methylated substrates reveals that TbPRMT7 is a type III PRMT, catalyzing the formation of only monomethylarginine, thereby representing the only exclusively type III PRMT identified to date. TbPRMT7 is expressed in both mammalian and insect stage T. brucei, and is apparently dispensable for growth in both life cycle stages. The enzyme is cytoplasmically localized, and is a component of several higher order complexes in vivo. Together, our studies indicate that TbPRMT7 is a Type III PRMT, and its robust activity and presence in numerous complexes suggest it plays multiple roles during the complex T. brucei life cycle.
PMID: 19254949 [PubMed - as supplied by publisher]
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Related Articles
- In vitro and in vivo analysis of the major type I protein arginine methyltransferase from Trypanosoma brucei. [Mol Biochem Parasitol. 2005]
- Evolutionarily divergent type II protein arginine methyltransferase in Trypanosoma brucei. [Eukaryot Cell. 2007]
- Arginine methylation of a mitochondrial guide RNA binding protein from Trypanosoma brucei. [Mol Biochem Parasitol. 2001]
- ReviewProtein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential. [Pharmacol Ther. 2007]
- ReviewInterplay between chromatin remodelers and protein arginine methyltransferases. [J Cell Physiol. 2007]
- 2: J Feline Med Surg. 2009 Feb 28. [Epub ahead of print]
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Specific anti-Leishmania spp. antibodies in stray cats in Greece.
Laboratory of Parasitology and Parasitic Diseases, Faculty of Veterinary Medicine, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece.
Greece is a highly endemic country for Leishmania species. Canine cases of leishmaniosis are recorded in different parts of the country. However, no case of feline leishmaniosis has been reported yet. In the present study, the seroprevalence in cats was investigated as a first approach to measuring Leishmania spp. infection of this animal species, in Greece. For this purpose, blood serum samples from 284 stray adult cats, living in the major area of Thessaloniki (Northern Greece), were examined by enzyme-linked immunosorbent assay for the detection of anti-Leishmania IgG. Eleven (3.87%) of the examined animals were found positive. The prevalence was lower in cats than in dogs coming from the same area, based on previous studies. Despite the low seroprevalence for Leishmania spp. in cats, leishmaniosis may be taken into consideration concerning the differential diagnosis of the feline diseases, especially in endemic areas.
PMID: 19254858 [PubMed - as supplied by publisher]
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- Review[Feline leishmaniasis: what's the epidemiological role of the cat?] [Parassitologia. 2004]
- Canine infection and the possible role of dogs in the transmission of American tegumentary leishmaniosis in Salta, Argentina. [Vet Parasitol. 2002]
- Feline leishmaniosis due to Leishmania infantum in Italy. [Vet Parasitol. 2002]
- Molecular diagnosis of leishmaniosis in dogs. Comparative application of traditional diagnostic methods and the proposed assay on clinical samples. [Vet Parasitol. 2003]
- Review[Problems and limitations of conventional and innovative methods for the diagnosis of Toxoplasmosis in humans and animals] [Parassitologia. 2004]
- 3: Biochem Biophys Res Commun. 2009 Feb 27. [Epub ahead of print]
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A 245kb mini-chromosome impacts on Leishmania braziliensis infection and survival.
Departamento de Biologia Celular, Instituto de Biologia Roberto Alcantara Gomes, Universidade do Estado do Rio de Janeiro, Rio de Janeiro, Brazil; Laboratório de Biologia Molecular de Parasitas e Vetores, Instituto Oswaldo Cruz, FIOCRUZ, Rio de Janeiro, Brazil.
Leishmania (V.) braziliensis, the causative agent of mucocutaneous leishmaniasis in the New World, may present an LD1 type genomic amplification that appears as a small 245kb linear chromosome, and is not clearly associated to the presence of a selection agent. A bt1 gene, codifying for a biopterin transporter protein, was identified in this small chromosome. Leishmania are auxotrophic for pterins and one of the proposed explanations for the appearance of this amplification is the improvement of biopterin capture by the parasite. We analyzed some biological aspects of two lineages of L. braziliensis strain M2903, with and without the small amplified chromosome. We showed differences in infectivity of these lineages, in macrophages and the insect vector Lutzomyia longipalpis, as well as in the uptake and metabolization of intermediates of the Leishmania biopterin salvage pathway. Our results suggest that the genomic amplification favors survival due to improved biopterin capture and at the same time hinders the infective capability, suggesting that within a population different parasites can perform different roles.
PMID: 19254695 [PubMed - as supplied by publisher]
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- The 245 kb amplified chromosome of Leishmania (V.) braziliensis contains a biopterin transporter gene. [Mem Inst Oswaldo Cruz. 2003]
- Testing of four Leishmania vaccine candidates in a mouse model of infection with Leishmania (Viannia) braziliensis, the main causative agent of cutaneous leishmaniasis in the New World. [Clin Vaccine Immunol. 2007]
- Leishmaniasis in Brazil: XVI. Isolation and identification of Leishmania species from sandflies, wild mammals and man in north Para State, with particular reference to L. braziliensis guyanensis causative agent of "pian-bois". [Trans R Soc Trop Med Hyg. 1981]
- ReviewAntiparasitic chemotherapy: tinkering with the purine salvage pathway. [Adv Exp Med Biol. 2008]
- ReviewThe role of dogs as reservoirs of Leishmania parasites, with emphasis on Leishmania (Leishmania) infantum and Leishmania (Viannia) braziliensis. [Vet Parasitol. 2007]
- 4: Enferm Infecc Microbiol Clin. 2009 Feb;27(2):136-7. Epub 2009 Feb 13.
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[Leishmaniasis: hospital and population-based incidence, and asymptomatic infection. A disease that is still with us.]
[Article in Spanish]Sección de Epidemiología, Centro de Salud Pública de Castellón, Castellón, CIBER de Epidemiología y Salud Pública, Barcelona, España.
PMID: 19254647 [PubMed - in process]
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- [Interpretation of laboratory data during cryptic leishmaniasis in dog] [Parassitologia. 2004]
- Review[Leishmaniasis and human immunodeficiency virus: an emerging co-infection?] [Med Trop (Mars). 1999]
- Epidemiology and direct medical costs of human leishmaniasis in Italy. [J Prev Med Hyg. 2007]
- Comparison of active and passive case detection of cutaneous leishmaniasis in Guatemala. [Am J Trop Med Hyg. 1990]
- ReviewEpidemiology of sepsis: an update. [Crit Care Med. 2001]
- 5: Handb Exp Pharmacol. 2009;(190):77-92.
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In vitro analysis and modification of aquaporin pore selectivity.
Pharmaceutical Chemistry, University of Kiel, Gutenbergstrasse 76, Kiel, 24118, Germany. ebeitz@pharmazie.uni-kiel.de
Aquaporins enable the passage of a diverse set of solutes besides water. Many novel aquaporin permeants, such as antimonite and arsenite, silicon, ammonia, and hydrogen peroxide, have been described very recently. By the same token, the number of available aquaporin sequences has rapidly increased. Yet, sequence analyses and structure models cannot reliably predict permeability properties. Even the contribution to pore selectivity of individual residues in the channel layout is not fully understood. Here, we describe and discuss established in vitro assays for water and solute permeability. Measurements of volume change due to flux along osmotic or chemical gradients yield quantitative biophysical data, whereas phenotypic growth assays can hint at the relevance of aquaporins in the physiological setting of a certain cell. We also summarize data on the modification of pore selectivity of the prototypical water-specific mammalian aquaporin-1. We show that replacing residues in the pore constriction region allows ammonia, urea, glycerol, and even protons to pass the aquaporin pore.
PMID: 19096773 [PubMed - indexed for MEDLINE]
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Related Articles
- Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons. [Proc Natl Acad Sci U S A. 2006]
- ReviewAquaporins with selectivity for unconventional permeants. [Cell Mol Life Sci. 2007]
- ReviewAmmonia and urea permeability of mammalian aquaporins. [Handb Exp Pharmacol. 2009]
- A single aquaporin gene encodes a water/glycerol/urea facilitator in Toxoplasma gondii with similarity to plant tonoplast intrinsic proteins. [FEBS Lett. 2003]
- Rapid gating and anion permeability of an intracellular aquaporin. [Nature. 1999]
- 6: Nucleic Acids Res. 2009 Jan;37(Database issue):D544-9. Epub 2008 Oct 30.
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TcSNP: a database of genetic variation in Trypanosoma cruzi.
Instituto de Investigaciones Biotecnológicas, Universidad de San Martín - CONICET, San Martín, 1650, Argentina.
The TcSNP database (http://snps.tcruzi.org) integrates information on genetic variation (polymorphisms and mutations) for different stocks, strains and isolates of Trypanosoma cruzi, the causative agent of Chagas disease. The database incorporates sequences (genes from the T. cruzi reference genome, mRNAs, ESTs and genomic sequences); multiple sequence alignments obtained from these sequences; and single-nucleotide polymorphisms and small indels identified by scanning these multiple sequence alignments. Information in TcSNP can be readily interrogated to arrive at gene sets, or SNP sets of interest based on a number of attributes. Sequence similarity searches using BLAST are also supported. This first release of TcSNP contains nearly 170,000 high-confidence candidate SNPs, derived from the analysis of annotated coding sequences. As new sequence data become available, TcSNP will incorporate these data, mapping new candidate SNPs onto the reference genome sequences.
PMID: 18974180 [PubMed - indexed for MEDLINE]
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Related Articles
- TcruziDB: an integrated Trypanosoma cruzi genome resource. [Nucleic Acids Res. 2004]
- CASCAD: a database of annotated candidate single nucleotide polymorphisms associated with expressed sequences. [BMC Genomics. 2005]
- Database of Trypanosoma cruzi repeated genes: 20,000 additional gene variants. [BMC Genomics. 2007]
- A random sequencing approach for the analysis of the Trypanosoma cruzi genome: general structure, large gene and repetitive DNA families, and gene discovery. [Genome Res. 2000]
- ReviewSingle nucleotide polymorphism in transcriptional regulatory regions and expression of environmentally responsive genes. [Toxicol Appl Pharmacol. 2005]
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