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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-1-15
pubmed:abstractText
The eggs of Schistosoma mansoni express a plethora of glycoconjugate antigens. A specific subset of these antigens can be detected in the serum or urine of infected individuals by a diagnostic sandwich ELISA using the anti-carbohydrate monoclonal antibody (mAb) 114-4D12-A [Nourel Din MS, Nibbeling R, Rotmans JP, Polderman AM, Krijger FW, Deelder AM. Quantitative determination of circulating soluble egg antigen in urine and serum of Schistosoma mansoni-infected individuals using a combined two-site enzyme-linked immunosorbent assay. Am J Trop Med Hyg 1994;50:585-94]. We used affinity chromatography to isolate the 114-4D12-binding glycoprotein subset from soluble egg antigens (SEA) of S. mansoni. SEA and the isolated SEA-subset (SEA-4D12) were subjected to reductive beta-elimination and hydrazinolysis to release intact glycans and glycan fragments, respectively, from the protein backbones. The released glycans were characterised by matrix-assisted laser-desorption-ionisation time-of-flight (MALDI-TOF) mass spectrometry (MS), liquid-chromatography (LC)-MS and gas chromatography (GC)-MS linkage analysis. Glycans released by reductive beta-elimination from SEA-4D12 were larger and more heavily fucosylated than glycans released from SEA. Most SEA-4D12 glycans contained a branched O-glycan core structure carrying up to 4 N-acetylhexosamines per chain which were substituted with maximum 12 fucose residues. Hydrazinolysis of SEA-4D12 resulted in the release of fucosylated antenna fragments. After 2-aminobenzamide (2AB)-labelling these fragments were subjected to 114-4D12-affinity purification. Normal phase (NP)-LC analysis of the flow-through and retained fractions indicated that the Fucalpha1-2Fucalpha1-3GalNAcbeta1-4(Fucalpha1-2Fucalpha1-3)GlcNAcbeta1- element forms the epitope of mAb 114-4D12. Most O-glycans from SEA-4D12 contain this structural element. Epitope-bearing N-glycans have not been found. In terms of abundance in total SEA, only a minority of all glycans possesses the epitope. This multifucosylated motif has so far only been found in schistosomes, providing a structural basis for the high specificity of the diagnostic antibody.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
148-61
pubmed:meshHeading
pubmed-meshheading:17188765-Animals, pubmed-meshheading:17188765-Antibodies, Helminth, pubmed-meshheading:17188765-Antibodies, Monoclonal, pubmed-meshheading:17188765-Antigens, Helminth, pubmed-meshheading:17188765-Carbohydrate Conformation, pubmed-meshheading:17188765-Carbohydrate Sequence, pubmed-meshheading:17188765-Chromatography, Affinity, pubmed-meshheading:17188765-Epitopes, pubmed-meshheading:17188765-Fucose, pubmed-meshheading:17188765-Glycoproteins, pubmed-meshheading:17188765-Hydrazines, pubmed-meshheading:17188765-Molecular Sequence Data, pubmed-meshheading:17188765-Ovum, pubmed-meshheading:17188765-Oxidation-Reduction, pubmed-meshheading:17188765-Polysaccharides, pubmed-meshheading:17188765-Schistosoma mansoni, pubmed-meshheading:17188765-Spectrometry, Mass, Matrix-Assisted Laser...
pubmed:year
2007
pubmed:articleTitle
Targeted identification of a unique glycan epitope of Schistosoma mansoni egg antigens using a diagnostic antibody.
pubmed:affiliation
Department of Parasitology, Centre of Infectious Diseases, Leiden University Medical Centre, P.O. Box 9600, 2300 RC Leiden, The Netherlands.
pubmed:publicationType
Journal Article