What's new for 'Trypanosomatids' in PubMed

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Sent on Wednesday, 2011 Apr 06
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 - 6 of 6

1.	Protein Sci. 2011 Apr 4. doi: 10.1002/pro.631. [Epub ahead of print] Crystal structure of the Leishmania major MIX protein: A scaffold protein that mediates protein-protein interactions. Gorman MA, Uboldi AD, Walsh PJ, Tan KS, Hansen G, Huyton T, Ji H, Curtis J, Kedzierski L, Papenfuss2 AT, Dogovski C, Perugini MA, Simpson RJ, Handman E, Parker MW. Biota Structural Biology Laboratory, St. Vincent's Institute of Medical Research, Victoria 3065, Australia. Abstract Infection by Leishmania and Trypanosoma cause severe disease and can be fatal. The reduced effectiveness of current treatments is largely due to drug resistance hence the urgent need to develop new drugs, preferably against novel targets. We have recently identified a mitochondrial membrane-anchored protein, designated MIX, which occurs exclusively in these parasites and is essential for virulence. We have determined the crystal structure of Leishmania major MIX to a resolution of 2.4 Å. MIX forms an all α-helical fold comprising seven α-helices that fold into a single domain. The distribution of helices is similar to a number of scaffold proteins, namely HEAT repeats, 14-3-3 and Tetratricopeptide Repeat proteins, suggesting that MIX mediates protein-protein interactions. Accordingly, employing co-purification and mass spectroscopy we were able to identify several proteins that may interact with MIX in vivo. Being parasite-specific, MIX is a promising new drug target and thus the structure and potential interacting partners provide a basis for structure guided drug discovery. Copyright © The Protein Society.
	PMID: 21465610 [PubMed - as supplied by publisher]
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2.	Bioinformation. 2011 Mar 2;6(1):20-2. A comparative protein function analysis databaseof different Leishmania strains. Dikhit MR, Nathasharma YP, Patel L, Rana SP, Sahoo GC, Das P. BioMedical Informatics Division, Rajendra Memorial Research Institute of Medical Sciences (RMRIMS), Agam kuan, Patna-800007, India. Abstract A complete understanding of different protein functional families and template information opens new avenues for novel drug development. Protein identification and analysis software performs a central role in the investigation of proteins and leads to the development of refined database for description of proteins of different Leishmania strains. There are certain databases for different strains that lack template information and functional family annotation. Rajendra Memorial Research Institute of Medical Sciences (RMRIMS) has developed a web-based unique database to provide information about functional families of different proteins and its template information in different Leishmania species. Based on the template information users can model the tertiary structure of protein. The database facilitates significant relationship between template information and possible protein functional families assigned to different proteins by SVMProt. This database is designed to provide comprehensive descriptions of certain important proteins found in four different species of Leishmania i.e. L. donovani, L. infantum, L. major and L. braziliensis. A specific characterization information table provides information related to species and specific functional families. This database aims to be a resource for scientists working on proteomics. The database is freely available at http://biomedinformri.org/calp/.
	PMID: 21464840 [PubMed - in process]
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3.	Antimicrob Agents Chemother. 2011 Apr 4. [Epub ahead of print] Antimony resistant clinical isolates of Leishmania donovani are susceptible to paromomycin and sitamaquine. Kulshrestha A, Singh R, Kumar D, Negi NS, Salotra P. Institute of Pathology (ICMR), Safdarjung Hospital Campus, New Delhi-110029, India; Safdarjung Hospital and Vardhman Mahavir Medical College, New Delhi-110029, India. Abstract Widespread antimonial resistance in anthroponotic visceral leishmaniasis (VL) makes it critical to monitor susceptibility of prevailing field isolates towards upcoming anti-leishmanials for framing the right treatment policies to protect these drugs against development of resistance. We aimed to generate the baseline data on natural in vitro susceptibility towards paromomycin and sitamaquine in Leishmania donovani field isolates from VL patients (n=20) belonging to zones of varying sodium antimony gluconate (SAG) resistance. We further monitored nitric oxide (NO) release in infected macrophages treated with these drugs. Field isolates exhibited a variable sensitivity to paromomycin and sitamaquine with respective mean ED50±SEMof 3.9±0.3μM and 2.1±0.2μM at intracellular amastigote stage and 29.8±2.5 μM and 17.7±1.0μM at promastigote stage. Susceptibility at the two parasite stages did not correlate for either drug. Isolates from high SAG resistance zone exhibited significantly lower susceptibility for sitamaquine in comparison to those from low SAG resistance zone, while isolates from different zones showed similar susceptibility to paromomycin. NO release was promoted in L.donovani infected macrophages upon treatment with paromomycin/sitamaquine. NO inhibitor significantly compromised the amastigote killing by sitamaquine but not by paromomycin. In conclusion, SAG resistant/sensitive VL isolates were susceptible to both paromomycin and sitamaquine. Paromomycin, exhibiting higher efficacy towards SAG resistant parasites and having a distinct mechanism of action, appears a promising drug for combination therapy.
	PMID: 21464251 [PubMed - as supplied by publisher]
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4.	Rev Soc Bras Med Trop. 2010 Oct;43(5):483-5. [Centenary of the discovery of Chagas disease: challenges and prospects]. [Article in Portuguese] Malafaia G, Rodrigues AS. Free Article
	PMID: 21085853 [PubMed - indexed for MEDLINE]
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5.	Rev Inst Med Trop Sao Paulo. 2010 Oct;52(5):269-72. Epidemiological investigation of an acute case of Chagas d isease in an area of active transmission in Peruvian Amazon region. Cabrera R, Vega S, Cáceres AG, Ramal AC, Alvarez C, Ladera P, Pinedo R, Chuquipiondo G. Grupo Temático de Enfermedades Metaxénicas, Dirección General de Epidemiología, Ministerio de Salud, Lima, Perú. Abstract The study objective was to investigate an acute case of Chagas disease in the San Pedro de Shishita community, Pebas District, in the Peruvian Amazon basin, a non-endemic area. Both parents of the index case (acute case) were thoroughly interviewed, a seroepidemiological survey was carried out in the community, parasitological exams were carried out only in relatives of the index case, and triatomine bugs were searched for inside houses, peridomiciliary, and in wild environments. Seroprevalence for IgG anti-T. cruzi antibodies was 1/104 (0.96%), using an ELISA test and an indirect immunofluorescence assay. Panstrongylus geniculatus and Rhodnius pictipes adults were found. The index case is autochthonous from San Pedro de Shishita, but the source of transmission is unknown. Free Article
	PMID: 21049232 [PubMed - indexed for MEDLINE]
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6.	Hum Immunol. 2010 Oct;71(10):964-7. Epub 2010 Jul 24. Increased levels of IgA antibodies against CRA and FRA recombinant antigens of Trypanosoma cruzi differentiate digestive forms of Chagas disease. Vasconcelos RH, Amaral FN, Cavalcanti MG, Silva ED, Ferreira AG, Morais CN, Gomes YM. Departamento de Imunologia, Instituto Aggeu Magalhães/Fiocruz, Recife, Pernambuco, Brazil. Abstract In the chronic phase of Chagas disease, individuals infected by Trypanosoma cruzi may be asymptomatic or may present cardiac and/or digestive complications. Our aim here was to analyze the relationship between the presence of specific immunoglobulin A antibodies and the different chronic clinical forms of Chagas disease using two recombinant antigens of Trypanosoma cruzi, cytoplasmatic repetitive antigen and flagellar repetitive antigen. The association of this immunoglobulin isotype with the digestive and cardio-digestive forms of the disease determined by indirect enzyme-linked immunosorbent assay, strongly suggests that IgA antibodies against these recombinant antigens of T. cruzi can be used as an immunological marker of the digestive alterations caused by Chagas disease. The tests performed in this study show that it is possible to differentiate digestive forms of Chagas disease. The knowledge provided by these results may help physicians to manage early alterations in the digestive tract of patients with the indeterminate or cardiac forms of Chagas disease. Prospective studies, however, with follow-up of the patients that presenting with high levels of immunoglobulin A against cytoplasmatic repetitive antigen and flagellar repetitive antigen recombinant antigens, need to be conducted to confirm this hypothesis. 2010 American Society for Histocompatibility and Immunogenetics. Published by Elsevier Inc. All rights reserved.
	PMID: 20659514 [PubMed - indexed for MEDLINE]
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