Analysis of the fine specificity of Tn-binding proteins using synthetic glycopeptide epitopes and a biosensor based on surface plasmon resonance spectroscopy

Authors
Osinaga, E Bay, S Tello, D Babino, A Pritsch, O Assemat, K Cantacuzene, D Nakada, H Alzari, P
Citation
E. Osinaga et al., Analysis of the fine specificity of Tn-binding proteins using synthetic glycopeptide epitopes and a biosensor based on surface plasmon resonance spectroscopy, FEBS LETTER, 469(1), 2000, pp. 24-28
Citations number
37
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
469
Issue
1
Year of publication
2000
Pages
24 - 28
Database
ISI
SICI code
0014-5793(20000303)469:1<24:AOTFSO>2.0.ZU;2-W
Abstract
Using synthetic Tn (GalNAc-O-Ser/Thr) glycopeptide models and a biosensor b ased on surface plasmon resonance spectroscopy we have determined that isol ectin B4 from Vicia villosa (VVLB4) binds to one Tn determinant whereas the anti-Tn monoclonal antibodies 83D4 and MLS128 require at least two Tn resi dues for recognition. When an unglycosylated amino acid is introduced betwe en the Tn residues, both antibodies do not bind. MLS128 affinity was higher on a glycopeptide with three consecutive Tn residues. These results indica te that Tn residues organized in clusters are essential for the binding of these antibodies and indicate a different Tn recognition pattern for VVLB4. (C) 2000 Federation of European Biochemical Societies.