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Identification and location on syndecan‐1 core protein of the epitopes of B‐B2 and B‐B4 monoclonal antibodies
Author(s) -
Dore Jean-Michel,
Morard Florence,
Vita Natalio,
Wijdenes John
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00310-x
Subject(s) - epitope , monoclonal antibody , syndecan 1 , mimotope , phage display , epitope mapping , antibody , microbiology and biotechnology , chemistry , b cell , glycosaminoglycan , biology , peptide , biochemistry , cell , immunology
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.