Linked Life Data

18439691

Source:http://linkedlifedata.com/resource/pubmed/id/18439691

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-5-26
pubmed:abstractText
The secretome of a parasite in its definitive host can be considered to be its genome in trans, to the extent that secreted products encoded by the parasite fulfill their function in the host milieu. The 'extended phenotype' of the filarial parasite, Brugia malayi, is of particular interest because of the evidence that infection results in potent down-modulation of the host immune response. We collected B. malayi 'excretory-secretory' (BES) proteins from adult parasites and using a combination of shotgun LC-MS/MS and 2D gel electrophoresis, identified 80 B. malayi and two host proteins in BES, of which 31 (38%) were detectable in whole worm extract (BmA). Products which were enriched in BES relative to BmA included phosphatidylethanolamine-binding protein (PEB), leucyl aminopeptidase (LAP, homologue of ES-62 from the related filaria Acanthocheilonema viteae), N-acetylglucosaminyltransferase (GlcNAcT) and galectin-1, in addition to the previously described major surface glycoprotein, glutathione peroxidase (gp29, GPX-1) and the cytokine homologue macrophage migration inhibitory factor (MIF-1). One of the most abundant released proteins was triose phosphate isomerase (TPI), yet many other glycolytic enzymes (such as aldolase and GAPDH) were found only in the somatic extract. Among the more prominent novel products identified in BES were a set of 11 small transthyretin-like proteins, and three glutamine-rich-repeat mucin-like proteins. Notably, no evidence was found of any secreted protein corresponding to the genome of the Wolbachia endosymbiont present in B. malayi. Western blotting with anti-phosphorylcholine (PC) monoclonal antibody identified that GlcNAcT, and not the ES-62 homologue, is the major PC-bearing protein in BES, while probing with human filariasis sera showed preferential reactivity to galectin-1 and to processed forms of myotactin. Overall, this analysis demonstrates selective release of a suite of newly identified proteins not previously suspected to be involved at the host-parasite interface, and provides important new perspectives on the biology of the filarial parasite.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
160
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-21
pubmed:meshHeading
pubmed-meshheading:18439691-Amino Acid Sequence, pubmed-meshheading:18439691-Animals, pubmed-meshheading:18439691-Blotting, Western, pubmed-meshheading:18439691-Brugia malayi, pubmed-meshheading:18439691-Chromatography, Liquid, pubmed-meshheading:18439691-Computational Biology, pubmed-meshheading:18439691-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:18439691-Filariasis, pubmed-meshheading:18439691-Galectins, pubmed-meshheading:18439691-Helminth Proteins, pubmed-meshheading:18439691-Humans, pubmed-meshheading:18439691-Macrophage Migration-Inhibitory Factors, pubmed-meshheading:18439691-Molecular Sequence Data, pubmed-meshheading:18439691-N-Acetylglucosaminyltransferases, pubmed-meshheading:18439691-Proteome, pubmed-meshheading:18439691-Proteomics, pubmed-meshheading:18439691-Spectrometry, Mass, Matrix-Assisted Laser...
pubmed:year
2008
pubmed:articleTitle
The secretome of the filarial parasite, Brugia malayi: proteomic profile of adult excretory-secretory products.
pubmed:affiliation
Institute of Immunology and Infection Research, University of Edinburgh, Ashworth Laboratories, Edinburgh,UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't