Abbott W M, Mellor A, Edwards Y, Feizi T
Section of Glycoconjugate Research, M.R.C. Clinical Research Centre, Harrow, Middx., U.K.
Biochem J. 1989 Apr 1;259(1):283-90. doi: 10.1042/bj2590283.
A full-length cDNA clone for the 13-14 kDa soluble beta-galactoside-binding lectin was isolated from a bovine fibroblast cDNA library. The derived amino acid sequence shows eight differences from a preliminary partial amino acid sequence given previously for the bovine heart lectin. This observation led to a re-examination of the data and correction of the heart lectin protein sequence. Except for a possible polymorphism of the heart lectin at position 57, the fibroblast and heart lectin sequences are considered identical. The epitope recognized by two monoclonal anti-(bovine lectin) antibodies, 36/8 and 9/5, was identified as the tetrapeptide sequence W-G-A/S-E/D by the isolation of several different cDNA clones from a human intestine cDNA library. A similar tetrapeptide is present in all of the soluble beta-galactoside-binding animal lectins sequenced thus far. It is also found in myelin basic protein, which we show is antigenically cross-reactive with the lectin. In myelin basic protein the tetrapeptide is a part of the major domain previously shown to be responsible for the induction of experimental allergic encephalomyelitis.
从牛成纤维细胞cDNA文库中分离出了编码13 - 14 kDa可溶性β-半乳糖苷结合凝集素的全长cDNA克隆。推导的氨基酸序列与先前给出的牛心脏凝集素初步部分氨基酸序列有8处差异。这一发现促使对数据进行重新检查并修正了心脏凝集素的蛋白质序列。除了心脏凝集素第57位可能存在多态性外，成纤维细胞凝集素和心脏凝集素序列被认为是相同的。通过从人肠道cDNA文库中分离出几个不同的cDNA克隆，确定了两种单克隆抗（牛凝集素）抗体36/8和9/5识别的表位为四肽序列W - G - A/S - E/D。到目前为止，在所有已测序的可溶性β-半乳糖苷结合动物凝集素中都存在类似的四肽。在髓鞘碱性蛋白中也发现了这种四肽，我们发现它与凝集素存在抗原交叉反应。在髓鞘碱性蛋白中，该四肽是先前已证明负责诱导实验性过敏性脑脊髓炎的主要结构域的一部分。
