Identification and location on syndecan-1 core protein of the epitopes of B-B2 and B-B4 monoclonal antibodies
| Autor: | Jean-Michel Dore, John Wijdenes, Natalio Vita, Florence Morard |
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| Rok vydání: | 1998 |
| Předmět: |
Syndecans
medicine.drug_class Molecular Sequence Data Biophysics Monoclonal antibody Biochemistry Peptide phage display Epitope B-B4 monoclonal antibody Syndecan 1 Antibody Specificity Peptide Library Structural Biology Genetics medicine Amino Acid Sequence Peptide library Molecular Biology Membrane Glycoproteins Linear epitope biology Chemistry Mimotope Epitope characterization Antibodies Monoclonal Cell Biology Molecular biology Recombinant Proteins carbohydrates (lipids) Epitope mapping biology.protein Proteoglycans Syndecan-1 B-B2 monoclonal antibody Antibody Peptides Epitope Mapping |
| Zdroj: | FEBS Letters. 426:67-70 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(98)00310-x |
| Popis: | Using a phage display peptide library, we characterized the epitope of two monoclonal antibodies reacting with syndecan-1: B-B2 and B-B4. The identified epitopes QDIT, for B-B2, and LPEV, for B-B4, were found to align with residues 36–39 and 90–93 of the mature protein, respectively. In contrast to B-B4, the B-B2 epitope is close to a potential glycosaminoglycan attachment site. Since syndecan-1 is heavily glycosylated and post-translational modifications are cell type specific, these results might explain the differences observed in the reactivity pattern of B-B2 and B-B4 and suggest that these monoclonal antibodies are useful probes to study cell surface exposed syndecan-1. |
| Databáze: | OpenAIRE |
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