Related Articles1H-NMR metabolite profiles of different strains of Plasmodium falciparum.
Biosci Rep. 2014;34(6):e00150
Authors: Teng R, Lehane AM, Winterberg M, Shafik SH, Summers RL, Martin RE, van Schalkwyk DA, Junankar PR, Kirk K
Abstract
Although efforts to understand the basis for inter-strain phenotypic variation in the most virulent malaria species, Plasmodium falciparum, have benefited from advances in genomic technologies, there have to date been few metabolomic studies of this parasite. Using 1H-NMR spectroscopy, we have compared the metabolite profiles of red blood cells infected with different P. falciparum strains. These included both chloroquine-sensitive and chloroquine-resistant strains, as well as transfectant lines engineered to express different isoforms of the chloroquine-resistance-conferring pfcrt (P. falciparum chloroquine resistance transporter). Our analyses revealed strain-specific differences in a range of metabolites. There was marked variation in the levels of the membrane precursors choline and phosphocholine, with some strains having >30-fold higher choline levels and >5-fold higher phosphocholine levels than others. Chloroquine-resistant strains showed elevated levels of a number of amino acids relative to chloroquine-sensitive strains, including an approximately 2-fold increase in aspartate levels. The elevation in amino acid levels was attributable to mutations in pfcrt. Pfcrt-linked differences in amino acid abundance were confirmed using alternate extraction and detection (HPLC) methods. Mutations acquired to withstand chloroquine exposure therefore give rise to significant biochemical alterations in the parasite.
[NMR paper] NMR assignment of the immune mapped protein 1 (IMP1)*homologue from Plasmodium falciparum.
NMR assignment of the immune mapped protein 1 (IMP1)*homologue from Plasmodium falciparum.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR assignment of the immune mapped protein 1 (IMP1)*homologue from Plasmodium falciparum.
Biomol NMR Assign. 2015 May 7;
Authors: Benjamin S, Williams F, Kerry L, Matthews S
Abstract
Plasmodium falciparum is responsible for causing cerebral malaria in humans. IMP1 is an immunogenic protein,...
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05-08-2015 09:18 PM
[NMR paper] Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum.
Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum.
Related Articles Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum.
Acta Crystallogr F Struct Biol Commun. 2015 May 1;71(Pt 5):514-521
Authors: Buchko GW, Yee A, Semesi A, Myler PJ, Arrowsmith CH, Hui R
Abstract
Protozoa of the genus Plasmodium are responsible for malaria, which is perhaps the most important parasitic disease to infect mankind. The emergence of...
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05-07-2015 03:04 PM
[NMR paper] Ligand-induced conformational change of Plasmodium falciparum AMA1 detected using (19)F NMR.
Ligand-induced conformational change of Plasmodium falciparum AMA1 detected using (19)F NMR.
Related Articles Ligand-induced conformational change of Plasmodium falciparum AMA1 detected using (19)F NMR.
J Med Chem. 2014 Jul 28;
Authors: Ge X, MacRaild CA, Devine S, Debono CO, Wang G, Scammells PJ, Scanlon MJ, Anders RF, Foley M, Norton RS
Abstract
We established an efficient means of probing ligand-induced conformational change in the malaria drug target AMA1 using 19F NMR. AMA1 was labeled with 5-fluorotryptophan (5F-Trp) and...
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07-30-2014 10:22 AM
[NMR paper] Application of Two-Dimensional NMR Spectroscopy to Metabotyping Laboratory Escherichia coli Strains.
Application of Two-Dimensional NMR Spectroscopy to Metabotyping Laboratory Escherichia coli Strains.
Related Articles Application of Two-Dimensional NMR Spectroscopy to Metabotyping Laboratory Escherichia coli Strains.
Chem Biodivers. 2013 Oct;10(10):1816-1827
Authors: Chae YK, Kim SH, Nam YK
Abstract
NMR Spectroscopy has been established as a major tool for identification and quantification of metabolites in a living system. Since the metabolomics era began, one-dimensional NMR spectroscopy has been intensively employed due to its...
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10-17-2013 04:57 PM
Ammonia Channeling in Plasmodium falciparum GMP Synthetase: Investigation by NMR Spectroscopy and Biochemical Assays
Ammonia Channeling in Plasmodium falciparum GMP Synthetase: Investigation by NMR Spectroscopy and Biochemical Assays
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1017057/aop/images/medium/bi-2010-017057_0002.gif
Biochemistry
DOI: 10.1021/bi1017057
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04-01-2011 09:31 PM
[NMR paper] Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surf
Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-1(19) mapped by TROSY NMR.
Related Articles Malaria parasite-inhibitory antibody epitopes on Plasmodium falciparum merozoite surface protein-1(19) mapped by TROSY NMR.
Mol Biochem Parasitol. 2004 Nov;138(1):29-36
Authors: Morgan WD, Lock MJ, Frenkiel TA, Grainger M, Holder AA
Plasmodium falciparum merozoite surface protein 1 (MSP1)(19), the C-terminal fragment of merozoite surface protein 1, is a leading candidate antigen for development of a...
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11-24-2010 10:03 PM
[NMR paper] Analysis of a Plasmodium falciparum EBA-175 peptide with high binding capacity to ery
Analysis of a Plasmodium falciparum EBA-175 peptide with high binding capacity to erythrocytes and their analogues using 1H NMR.
Related Articles Analysis of a Plasmodium falciparum EBA-175 peptide with high binding capacity to erythrocytes and their analogues using 1H NMR.
J Struct Biol. 2003 Feb;141(2):115-21
Authors: Cifuentes G, Guzmán F, Alba MP, Salazar LM, Patarroyo ME
A 175-erythrocyte-binding protein (EBA-175) conserved high-activity binding peptide (HABP), called 1783 (nonimmunogenic, nonprotective against Plasmodium falciparum...
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11-24-2010 09:01 PM
[NMR paper] NMR structure of Plasmodium falciparum malaria peptide correlates with protective imm
NMR structure of Plasmodium falciparum malaria peptide correlates with protective immunity.
Related Articles NMR structure of Plasmodium falciparum malaria peptide correlates with protective immunity.
Biochim Biophys Acta. 2002 May 10;1571(1):27-33
Authors: Purmova J, Salazar LM, Espejo F, Torres MH, Cubillos M, Torres E, Lopez Y, Rodríguez R, Patarroyo ME
Apical membrane antigen-1 is an integral Plasmodium falciparum malaria parasite membrane protein. High activity binding peptides (HABPs) to human red blood cells (RBCs) have been identified...