Division of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, 981-8558, Japan,
Fish Physiol Biochem. 2013 Dec;39(6):1619-30. doi: 10.1007/s10695-013-9814-6. Epub 2013 Jun 6.
Osmerus (Spirinchus) lanceolatus egg lectin (OLL) is a member of the rhamnose-binding lectin (RBL) family which is mainly found in aqueous beings. cDNA of OLL was cloned, and its genomic architecture was revealed. The deduced amino acid (aa) sequence indicated that OLL was composed of 213 aa including 95 aa of domain N and 97 aa of domain C. N and C showed 73 % sequence identity and contained both -ANYGR- and -DPC-KYL-peptide motifs which are conserved in most of the RBL carbohydrate recognition domains. The calculated molecular mass of mature OLL was 20,852, consistent with the result, and 20,677.716, from mass spectrometry. OLL was encoded by eight exons: exons 1 and 2 for a signal peptide; exons 3-5 and 6-8 for N- and C-domains, respectively. Surface plasmon resonance spectrometric analyses revealed that OLL showed comparable affinity for Galα- and β-linkages, whereas Silurus asotus lectin (SAL), a catfish RBL, bound preferentially to α-linkages of neoglycoproteins. The Kd values of OLL and SAL against globotriaosylceramide (Gb3) were 1.69 × 10⁻⁵ M for and 2.81 × 10⁻⁶ M, respectively. Thus, the carbohydrate recognition property of OLL is slightly different from that of SAL. On the other hand, frontal affinity chromatography revealed that both OLL and SAL interacted with only glycolipid-type oligosaccharides such as Gb3 trisaccharides, not with N-linked oligosaccharides. The domain composition of these RBLs and an analytical environment such as the "cluster effect" of a ligand might influence the binding between RBL and sugar chains.
尖吻拟鲿卵 lectin (OLL) 是 Rh 糖结合 lectin (RBL) 家族的一员，主要存在于水生生物中。克隆了 OLL 的 cDNA，并揭示了其基因组结构。推导的氨基酸 (aa) 序列表明，OLL 由 213 个 aa 组成，包括 95 个 aa 的 N 结构域和 97 个 aa 的 C 结构域。N 和 C 显示出 73%的序列同一性，并包含大多数 RBL 糖识别结构域中保守的 -ANYGR- 和 -DPC-KYL-肽基序。成熟 OLL 的计算分子质量为 20852，与质谱结果一致，为 20677.716。OLL 由 8 个外显子编码：外显子 1 和 2 为信号肽；外显子 3-5 和 6-8 分别为 N 结构域和 C 结构域。表面等离子体共振光谱分析表明，OLL 对 Galα-和 β-键具有相当的亲和力，而鲶鱼 RBL（SAL）则优先结合糖蛋白的α-键。OLL 和 SAL 对神经节苷脂三糖 (Gb3) 的 Kd 值分别为 1.69×10⁻⁵ M 和 2.81×10⁻⁶ M。因此，OLL 的糖识别特性与 SAL 略有不同。另一方面，前沿亲和层析表明，OLL 和 SAL 仅与糖脂型寡糖（如 Gb3 三糖）相互作用，而不与 N 连接的寡糖相互作用。这些 RBL 的结构域组成和分析环境（如配体的“聚集效应”）可能会影响 RBL 与糖链的结合。
