Dore J M, Morard F, Vita N, Wijdenes J
Diaclone, 1 bvd. A. Fleming, Besançon, France.
FEBS Lett. 1998 Apr 10;426(1):67-70. doi: 10.1016/s0014-5793(98)00310-x.
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.
利用噬菌体展示肽库,我们鉴定了两种与syndecan-1反应的单克隆抗体(B-B2和B-B4)的表位。已确定B-B2的表位为QDIT,B-B4的表位为LPEV,分别与成熟蛋白的第36 - 39位和第90 - 93位残基相对应。与B-B4不同,B-B2表位靠近一个潜在的糖胺聚糖附着位点。由于syndecan-1高度糖基化且翻译后修饰具有细胞类型特异性,这些结果可能解释了在B-B2和B-B4反应模式中观察到的差异,并表明这些单克隆抗体是研究细胞表面暴露的syndecan-1的有用探针。