Abstract |
The aim of the present study was the characterization of the dominant epitope present on Schistosoma mansoni glycolipids, which causes cross-reactivity of S. mansoni and S. haematobium infection sera with keyhole-limpet haemocyanin (KLH). To this end, the monoclonal antibody M2D3H was chosen for its similar behaviour in high-performance TLC immunostaining and inhibition-ELISA to infection sera. Individual, structurally defined oligosaccharides derived from S. mansoni egg glycolipids were tested for their binding to this monoclonal antibody by immunoaffinity chromatography. A terminal fucose residue linked in the (alpha1-->3) position to N- acetylgalactosamine was found to be the common structural determinant of the four oligosaccharides binding to M2D3H. The Fuc(alpha1-->3)GalNAc-motif also appeared to be the basis for the cross-reactivity with KLH, a phenomenon used in the serodiagnosis of S. mansoni, S. haematobium and S. japonicum infections.
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Authors | Sven R Kantelhardt, Manfred Wuhrer, Roger D Dennis, Michael J Doenhoff, Quentin Bickle, Rudolf Geyer |
Journal | The Biochemical journal
(Biochem J)
Vol. 366
Issue Pt 1
Pg. 217-23
(Aug 15 2002)
ISSN: 0264-6021 [Print] England |
PMID | 11996672
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Antigens
- Glycolipids
- Oligosaccharides
- Polysaccharides
- fucosyl alpha 1,3 N-acetylglucosamine
- Acetylglucosamine
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Topics |
- Acetylglucosamine
(analogs & derivatives, chemistry)
- Amino Acid Motifs
- Animals
- Antibody Specificity
- Antigens
(chemistry)
- Chromatography, Thin Layer
- Enzyme-Linked Immunosorbent Assay
- Glycolipids
(chemistry)
- Oligosaccharides
(chemistry)
- Polysaccharides
(chemistry)
- Protein Structure, Tertiary
- Schistosoma mansoni
(metabolism)
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Time Factors
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