Ma Y, Yokota Y, Kozutsumi Y, Kawasaki T
Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Biochem Mol Biol Int. 1996 Nov;40(5):965-74. doi: 10.1080/15216549600201593.
The serum mannan-binding protein (S-MBP) is a Ca(2+)-dependent C-type animal lectin specific for mannose and N-acetylglucosamine, which plays an important role in first-line host defense. To study the structure and function relationship of the lectin, a full-length human S-MBPcDNA was expressed in Sf9 insect cells using a baculovirus expression system, and a cDNA encoding the carbohydrate recognition domain (CRD) of human S-MBP was expressed in E. coli. The properties of the recombinant S-MBP and recombinant S-MBP-CRD were compared with those of the native human S-MBP and the CRD of the native S-MBP. The results indicated that functional human S-MBP can be successfully expressed in Sf9 cells and functional S-MBP-CRD in E. coli. In addition, the amino-terminal region and collagen-like domain are required for higher oligomer formation and play important roles in complement activation.
血清甘露聚糖结合蛋白（S-MBP）是一种对甘露糖和N-乙酰葡糖胺具有特异性的Ca(2+)依赖性C型动物凝集素，在宿主的一线防御中发挥重要作用。为了研究该凝集素的结构与功能关系，利用杆状病毒表达系统在Sf9昆虫细胞中表达了全长人S-MBP cDNA，并在大肠杆菌中表达了编码人S-MBP碳水化合物识别结构域（CRD）的cDNA。将重组S-MBP和重组S-MBP-CRD的特性与天然人S-MBP和天然S-MBP的CRD的特性进行了比较。结果表明，功能性人S-MBP可在Sf9细胞中成功表达，功能性S-MBP-CRD可在大肠杆菌中成功表达。此外，氨基末端区域和胶原样结构域对于形成更高的寡聚体是必需的，并且在补体激活中起重要作用。
