What's new for 'Trypanosomatids' in PubMed

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Sent on Thursday, 2010 Oct 21
Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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PubMed Results

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1.	Proteomics. 2010 Sep 9. [Epub ahead of print] Identification of Leishmania-specific protein phosphorylation sites by LC-ESI-MS/MS and comparative genomics analyses. Hem S, Gherardini PF, Fortéa JO, Hourdel V, Morales MA, Watanabe R, Pescher P, Kuzyk MA, Smith D, Borchers CH, Zilberstein D, Helmer-Citterich M, Namane A, Späth GF. Institut Pasteur, Plate-forme de Protéomique and CNRS URA 2185, Department of Structural Biology and Chemistry, Pasteur-Genopole Ile-de-France, Paris, France. Abstract Human pathogenic protozoa of the genus Leishmania undergo various developmental transitions during the infectious cycle that are triggered by changes in the host environment. How these parasites sense, transduce, and respond to these signals is only poorly understood. Here we used phosphoproteomic approaches to monitor signaling events in L. donovani axenic amastigotes, which may be important for intracellular parasite survival. LC-ESI-MS/MS analysis of IMAC-enriched phosphoprotein extracts identified 445 putative phosphoproteins in two independent biological experiments. Functional enrichment analysis allowed us to gain insight into parasite pathways that are regulated by protein phosphorylation and revealed significant enrichment in our data set of proteins whose biological functions are associated with protein turn-over, stress response, and signal transduction. LC-ESI-MS/MS analysis of TiO(2)-enriched phosphopeptides confirmed these results and identified 157 unique phosphopeptides covering 181 unique phosphorylation sites in 126 distinct proteins. Investigation of phosphorylation site conservation across related trypanosomatids and higher eukaryotes by multiple sequence alignment and cluster analysis revealed L. donovani-specific phosphoresidues in highly conserved proteins that share significant sequence homology to orthologs of the human host. These unique phosphorylation sites reveal important differences between host and parasite biology and post-translational protein regulation, which may be exploited for the design of novel anti-parasitic interventions.
	PMID: 20960452 [PubMed - as supplied by publisher]

2.	Trop Med Int Health. 2010 Oct 19. doi: 10.1111/j.1365-3156.2010.02642.x. [Epub ahead of print] Matrix metalloproteinase-9 and intercellular adhesion molecule 1 are powerful staging markers for human African trypanosomiasis. Hainard A, Tiberti N, Robin X, Ngoyi DM, Matovu E, Enyaru JC, Müller M, Turck N, Ndung'u JM, Lejon V, Sanchez JC.  Biomedical Proteomics Research Group, Medical University Centre, Geneva, Switzerland  Institut National de Recherche Biomédicale, Kinshasa, Congo  Department of Veterinary Parasitology and Microbiology, Faculty of Veterinary Medicine, Makerere University, Kampala, Uganda  Department of Biochemistry, Faculty of Science, Makerere University, Kampala, Uganda  Swiss Institute of Bioinformatics, Medical University Centre, Geneva, Switzerland  Foundation for Innovative New Diagnostics (FIND), Geneva, Switzerland  Department of Parasitology, Institute of Tropical Medicine, Antwerp, Belgium. Abstract Objectives  A critical step before treatment of human African trypanosomiasis (HAT) is the correct staging of the disease. As late stage is established when trypanosomes cross the blood-brain barrier and invade the central nervous system, we hypothesized that matrix metalloproteinases and cell adhesion molecules could indicate, alone or in combination, the disease progression from the first to the second stage of HAT. Methods  We measured the levels of MMP-2, MMP-9, ICAM-1, VCAM-1 and E-selectin in the cerebrospinal fluid (CSF) of 63 Trypanosoma brucei gambiense-infected patients (15 stage 1 and 48 stage 2). Staging was based on counting of white blood cells (WBC) and/or parasite detection in CSF. Concentrations were obtained either by ELISA or multiplex bead suspension assays, and results were compared with three known HAT staging markers (CXCL10, CXCL8 and H-FABP). Results  ICAM-1 and MMP-9 accurately discriminated between stage 1 and stage 2 patients with HAT with 95% sensitivity (SE) for 100% specificity (SP), which was better than CXCL10 (93% SE for 100% SP), one of the most promising known markers. Combination of ICAM-1 and MMP-9 with H-FABP provided a panel that resulted in 100% of SE and SP for staging HAT. Conclusions  ICAM-1 and MMP-9, alone or in combination, appeared as powerful CSF staging markers of HAT. Final validation of all newly discovered staging markers on a large multi-centric cohort including both forms of the disease as well as patients with others infections should be performed. © 2010 Blackwell Publishing Ltd.
	PMID: 20958893 [PubMed - as supplied by publisher]