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

FEBS Letters

Bay, Sylvie²  Tello, Diana³  Babino, Alvaro⁴  Osinaga, Eduardo⁴  Pritsch, Otto⁴  Assemat, Karine³  Cantacuzene, Daniele²  Nakada, Hiroshi¹  Alzari, Pedro³ 

[1] Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University, Kyoto 603, Japan;Unité de Chimie Organique, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris, France;Unité de Biochimie Structurale, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris, France;Departamento de Bioquı́mica, Facultad de Medicina, Av. Gral. Flores 2125, CP 11800 Montevideo, Uruguay

关键词: Tn antigen;    O-Glycosylation;    Lectin;    Monoclonal antibody;    Surface plasmon resonance spectroscopy;    Cancer;    mAb;    monoclonal antibody;    VVLB4;    isolectin B4 from Vicia villosa;   

DOI  :  10.1016/S0014-5793(00)01248-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using synthetic Tn (GalNAc-O-Ser/Thr) glycopeptide models and a biosensor based on surface plasmon resonance spectroscopy we have determined that isolectin B4 from Vicia villosa (VVLB4) binds to one Tn determinant whereas the anti-Tn monoclonal antibodies 83D4 and MLS128 require at least two Tn residues for recognition. When an unglycosylated amino acid is introduced between the Tn residues, both antibodies do not bind. MLS128 affinity was higher on a glycopeptide with three consecutive Tn residues. These results indicate that Tn residues organized in clusters are essential for the binding of these antibodies and indicate a different Tn recognition pattern for VVLB4.

【 授权许可】

Unknown