The Column - September 2008 - (Page 8)

News The Column September 2008 News Worms help in identifying biomarkers of infection Three principal species of blood flukes of the parasitic worm, Schistosoma, infect over 200 million people worldwide via infested water or penetration of the skin. At least 10 species have adverse effects on animal health including cattle, sheep and goats, causing serious difficulties for farmers and indigenous peoples. The worm can survive for long periods of time and has evolved defence mechanisms to evade the immune system of the host animal. The tegument, a structure covering the parasite’s outer surface, serves as an interface between the host and the parasite. This surface is where scientists are targeting anti-schistosome drugs and vaccines. Researchers in Spain including Ana Oleaga from the Institute of Natural Resources and Agrobiology of Salamanca have undertaken a proteomic study of the tegumental proteins of male and female S. bovis worms, which infect animals. The work has been reported in the journal Molecular & Biochemical Parasitology and comprised three digestion protocols.1 The most gentle procedure involved tryptic digestion for 30 minutes and the tegument appeared to have no breaks and no nuclear and mitochondrial proteins were detected but some cytosolic proteins present indicated the surface may have been penetrated. The proteins were identified using LC–MS of the peptide mixtures, followed by database searching. Many of those found were newly identified in S. bovis having a variety of functions including catalytic, cytoskeletal, binding functions and chaperone processes. Immunofluorescence and confocal microscopy corroborated the experimental protocol and confirmed that glyceraldehydes-3-phosphate dehydrogenase (GAPDH) and action were present on the tegument area of males and females and enolase was found exclusively on the surface of male worms. Reference 1. Molecular & Biochemical Parasitology, 161, 112–123 (2008). Heart felt research to boost HDL levels Combined statin and niacin therapy partially reverses the changes in the protein composition seen in HDL3 in coronary artery disease subjects, according to a recent study. Using liquid chromatography–Fourier transform–mass spectrometry researchers analysed HDL3 isolated from six coronary artery disease sufferers, before and one year after combination therapy. Alterations in protein composition were detected by spectral counting and confirmed with extracted ion chromatograms. Published on-line earlier1 the scientists, led by Pattie S. Green PhD at the University of Washington’s Department of Medicine in Seattle, USA previously demonstrated that HDL3 in subjects with coronary artery disease is enriched in apolipoprotein E and that the lipoprotein carries a distinct protein cargo. This observation suggested to them that altered protein composition might affect the antiatherogenic and antiinflammatory properties of HDL. Their conclusions raise the possibility that quantifying the HDL proteome could provide insights into the therapeutic efficacy of antiatherosclerotic interventions. Reference 1. Circulation. 2008 8 Riko Pictures/Getty Images

Table of Contents for the Digital Edition of The Column - September 2008

The Column - September 2008
Market Trends and Analysis: Water Analysis and Testing
Incognito - Turn On, Tune In, Outsource...
Separation of Complex Peptide Samples Using Optimized Column Technology and 1D-LC Conditions
Diastereoselective Separation of Fenvalerate by Supercritical Fluid Chromatography with Tandem Columns
Q&A - Highly Sensitive

The Column - September 2008