Tuesday, April 10, 2012

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 - 4 of 4    (Display the 4 citations in PubMed)

1. Biochem Biophys Res Commun. 2012 Mar 29. [Epub ahead of print]

Identification and characterization of a novel Ribose 5-phosphate isomerase B from Leishmania donovani.

Kaur PK, Dinesh N, Soumya N, Babu NK, Singh S.

Source

Department of Biotechnology, National Institute of Pharmaceutical Education and Research, SAS Nagar, Mohali 160 062, Punjab, India.

Abstract

Leishmaniasis is a group of tropical diseases caused by protozoan parasites of the genus Leishmania. Due to the emergence of resistance to the available antileishmanial drugs there is an immediate need to identify molecular targets on which to base future treatment strategies. Ribose 5-phosphate isomerase (Rpi; EC 5.3.1.6) is a key enzyme of the pentose phosphate pathway (PPP) which catalyses the reversible aldose-ketose isomerization between Ribose 5-phosphate (R5P) and Ribulose 5-phosphate (Ru5P). It exists in two isoforms A and B. These two are completely unrelated enzymes catalyzing the same reaction. Analysis of the Leishmania infantum genome revealed that though the RpiB gene is present, RpiA homologs are completely absent. An absence of RpiBs in the genomes of higher animals makes this enzyme a possible target for the chemotherapy of Leishmaniasis. In this paper, we report for the first time the presence of B isoform of the Rpi enzyme in Leishmania donovani (LdRpiB) by cloning and molecular characterization of the enzyme. An amplified L. donovani RpiB gene is 519bp and encodes for a putative 172 amino acid protein with a molecular mass of ∼19kDa. An ∼19kDa protein with poly-His tag at the C-terminal end was obtained by heterologous expression of LdRpiB in Escherichia coli. The recombinant form of RpiB was obtained in soluble and active form. The LdRpiB exists as a dimer of dimers i.e. the tetramer form. The polyclonal antibody against Trypanosoma cruzi RpiB could detect a band of ∼19kDa with the purified recombinant RpiB as well as native RpiB from the L. donovani promastigotes. Recombinant RpiB obeys the classical Michaelis-Menten kinetics utilizing R5P as the substrate with a K(m) value of 2.4±0.6mM and K(cat) value of 30±5.2s(-1). Our study confirms the presence of Ribose 5-phosphate isomerase B in L. donovani and provides functional characterization of RpiB for further validating it as a potential drug target.

Copyright © 2012. Published by Elsevier Inc.

PMID: 22483752 [PubMed - as supplied by publisher]
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2. Parasit Vectors. 2012 Apr 7;5(1):71. [Epub ahead of print]

The origins of the trypanosome genome strains Trypanosoma brucei brucei TREU 927, T. b. gambiense DAL 972, T. vivax Y486 and T. congolense IL3000.

Gibson W.

Abstract

ABSTRACT: The genomes of several tsetse-transmitted African trypanosomes (Trypanosoma brucei brucei, T. b. gambiense, T. vivax, T. congolense) have been sequenced and are available to search online. The trypanosome strains chosen for the genome sequencing projects were selected because they had been well characterised in the laboratory, but all were isolated several decades ago. The purpose of this short review is to provide some background information on the origins and biological characterisation of these strains as a source of reference for future users of the genome data. With high throughput sequencing of many more trypanosome genomes in prospect, it is important to understand the phylogenetic relationships of the genome strains.

PMID: 22483376 [PubMed - as supplied by publisher]
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3. Biochem Biophys Res Commun. 2012 Feb 3;418(1):140-3. Epub 2012 Jan 8.

Molecular interaction of the first 3 enzymes of the de novo pyrimidine biosynthetic pathway of Trypanosoma cruzi.

Nara T, Hashimoto M, Hirawake H, Liao CW, Fukai Y, Suzuki S, Tsubouchi A, Morales J, Takamiya S, Fujimura T, Taka H, Mineki R, Fan CK, Inaoka DK, Inoue M, Tanaka A, Harada S, Kita K, Aoki T.

Source

Department of Molecular and Cellular Parasitology, Juntendo University Graduate School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan. tnara@juntendo.ac.jp

Abstract

The first 3 reaction steps of the de novo pyrimidine biosynthetic pathway are catalyzed by carbamoyl-phosphate synthetase II (CPSII), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), respectively. In eukaryotes, these enzymes are structurally classified into 2 types: (1) a CPSII-DHO-ATC fusion enzyme (CAD) found in animals, fungi, and amoebozoa, and (2) stand-alone enzymes found in plants and the protist groups. In the present study, we demonstrate direct intermolecular interactions between CPSII, ATC, and DHO of the parasitic protist Trypanosoma cruzi, which is the causative agent of Chagas disease. The 3 enzymes were expressed in a bacterial expression system and their interactions were examined. Immunoprecipitation using an antibody specific for each enzyme coupled with Western blotting-based detection using antibodies for the counterpart enzymes showed co-precipitation of all 3 enzymes. From an evolutionary viewpoint, the formation of a functional tri-enzyme complex may have preceded-and led to-gene fusion to produce the CAD protein. This is the first report to demonstrate the structural basis of these 3 enzymes as a model of CAD. Moreover, in conjunction with the essentiality of de novo pyrimidine biosynthesis in the parasite, our findings provide a rationale for new strategies for developing drugs for Chagas disease, which target the intermolecular interactions of these 3 enzymes.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID: 22245425 [PubMed - indexed for MEDLINE]
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4. Ocul Immunol Inflamm. 2011 Dec;19(6):385-96.

Ocular parasitoses and their immunology.

Hoti SL, Tandon V.

Source

Microbiology and Immunology Division, Vector Control Research Centre (ICMR), Medical Complex, Indira Nagar, Pondicherry, India.

Abstract

Parasitic infections of the eye are a major cause of ocular diseases in many parts of the globe. The causative agents of ocular parasitoses include several species of unicellular protozoan and metazoan helminth parasites, which have a natural predilection for and utilize the eye as their habitat. At times ocular invasion by accidental or uncommon parasites may result in infections of unusual nature. In this review the authors discuss the various parasitic causal agents of eye diseases and the current status of immunology against ocular parasitoses.

PMID: 22106905 [PubMed - indexed for MEDLINE]
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