Epitopic structure of Tn glycophorin A for an anti-Tn antibody (MLS 128)
| Autor: | Alan Mellors, Mizue Inoue, Nobuhiro Tanaka, I Funakoshi, Hiroshi Nakada, Ikuo Yamashina, Shigeyuki Fukui, Yoshito Numata |
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| Rok vydání: | 1993 |
| Předmět: |
Antigenicity
Sequence analysis Molecular Sequence Data macromolecular substances Sialidase Epitope Epitopes stomatognathic system Animals Humans Glycophorin Antigens Tumor-Associated Carbohydrate Amino Acid Sequence Glycophorins Mannheimia haemolytica Chromatography High Pressure Liquid Sheep Multidisciplinary biology Glycopeptides Mucins Antibodies Monoclonal Metalloendopeptidases Ovine Submaxillary Mucin Molecular biology Glycopeptide Biochemistry Chromatography Gel biology.protein Antibody Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 90:2495-2499 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.90.6.2495 |
| Popis: | Glycophorin A was digested with glycoprotease (Pasteurella haemolytica) and the digest was fractionated by a combination of high-pressure column chromatographies to produce the glycopeptides GPA-1 to GPA-6. Sequence analysis of the glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with the accepted structure. The glycopeptides thus obtained were treated with sialidase and beta-galactosidase. The Tn antigenicity, as assayed by the binding to a monoclonal anti-Tn antibody (MLS 128), was found exclusively in the glycopeptides including three (cluster I) or four (cluster II) consecutive residues of GalNAc-Ser/Thr, whereas the glycopeptide (GPA-2) containing two nonconsecutive GalNAc-Ser/Thr residues had practically no Tn antigenicity. The immunoreactivities of GPA-1 and GPA-3, containing both clusters I and II, and GPA-4, containing cluster II, were 63% (calcd. 67%), 81% (calcd. 86%), and 50% (calcd. 50%), respectively, of the immunoreactivity of GPA-5 or GPA-6, containing cluster I (the average being taken as the basis), based on the reactivity per GalNAc residue. These results indicate that clusters I and II react with the antibody to the same extent. The structure consisting of three consecutive glycosylated Ser/Thr residues may be essential for Tn antigenicity in the light of previous results for ovine submaxillary mucin. |
| Databáze: | OpenAIRE |
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