|Involvement of glycan chains in the antigenicity of Rapana thomasiana hemocyanin|Siddiqui, N.I.; Idakieva, K.; Demarsin, B.; Doumanova, L.; Compernolle, F.; Gielens, C. (2007). Involvement of glycan chains in the antigenicity of Rapana thomasiana hemocyanin. Biochem. Biophys. Res. Commun. 361(3): 705-711. dx.doi.org/10.1016/j.bbrc.2007.07.098
In: Biochemical and Biophysical Research Communications. ACADEMIC PRESS INC ELSEVIER SCIENCE: San Diego etc.. ISSN 0006-291X, more
antigenicity; Electrospray ionization-mass spectrometry; ELISA;gastropod; glycan; Rapana thomasiana; hemocyanin; mollusc
|Authors|| || Top |
- Siddiqui, N.I.
- Idakieva, K.
- Demarsin, B.
- Doumanova, L.
- Compernolle, F.
- Gielens, C.
Functional unit (FU) RtH2-e from Rapana thomasiana hemocyanin (Hc) was degraded into small fragments with chymotrypsin. The glycopeptides were separated from the non-glycosylated peptides by chromatography on Concanavalin-A–Sepharose and characterized by mass spectrometry. The glycan part of the glycopeptides (all with common peptide stretch of 14 amino acids) consists of the classical trimannosyl-N,N-diacetylchitobiose core for N-glycosylation, predominantly extended with a unique tetrasaccharide that is branched on fucose. In inhibition ELISA experiments, the glycopeptides interfered in the complex formation between FU RtH2-e and rabbit antibodies against Rapana Hc (about 30% of inhibition). The inhibition also was retained after treatment of the glycopeptides with pronase in order to completely destroy the peptide part. The inhibitory effect of the non-glycosylated peptides, on the other hand, was very low. This study thus demonstrates that the glycans attached to FU RtH2-e contribute to the antigenicity of Rapana Hc.