Fuc(alpha1-->3)GalNAc-: the major antigenic motif of Schistosoma mansoni glycolipids implicated in infection sera and keyhole-limpet haemocyanin cross-reactivity.
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.
| Item Type | Article |
|---|---|
| Keywords | immunoaffinity chromatography, serodiagnosis, trematode, parasite, Monoclonal-antibodies, carbohydrate epitopes, serological, differentiation, structural characterization, n-glycans, hemocyanin, japonicum, vaccine, glycosphingolipids, immunity, Acetylglucosamine, analogs & derivatives, chemistry, Amino Acid Motifs, Animal, 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, Support, Non-U.S. Gov't, Time Factors |
| ISI | 177642400024 |
Explore Further
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222754 (OA Location)
- 10.1042/BJ20011678 (DOI)
- 11996672 (PubMed)