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80L5C4表位与盘基网柄菌细胞粘附分子gp80的嗜同性结合位点重叠。

The 80L5C4 epitope overlaps with the homophilic binding site of the cell adhesion molecule gp80 of Dictyostelium.

作者信息

Wu X F, Kamboj R K, Gariepy J, Siu C H

机构信息

Banting and Best Department of Medical Research, University of Toronto, Ont., Canada.

出版信息

Biochem Cell Biol. 1992 Mar-Apr;70(3-4):246-9. doi: 10.1139/o92-037.

Abstract

The monoclonal antibody (mAb) 80L5C4 is a potent inhibitor of the cell adhesion molecule gp80 of Dictyostelium discoideum. To map the exact location of the epitope recognized by mAb 80L5C4, overlapping hexapeptides were synthesized on plastic pins and the binding p6 mAb 80L5C4 to these peptides was monitored by enzyme-linked immunosorbent assay. The 80L5C4 epitope is mapped to a single hexapeptide sequence GYKLNV, which shares five amino acid residues with the octapeptide sequence YKLNVNDS involved in gp80 homophilic binding. Analogue studies indicate that the hydrophobic residues within this sequence are crucial for antigen recognition.

摘要

单克隆抗体(mAb)80L5C4是盘基网柄菌细胞粘附分子gp80的强效抑制剂。为了确定mAb 80L5C4识别的表位的确切位置,在塑料针上合成了重叠六肽,并通过酶联免疫吸附测定监测mAb 80L5C4与这些肽的结合。80L5C4表位被定位到单一的六肽序列GYKLNV,该序列与参与gp80同源结合的八肽序列YKLNVNDS共有五个氨基酸残基。类似物研究表明,该序列内的疏水残基对于抗原识别至关重要。

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