Structural and functional roles of the amino-terminal region and collagen-like domain of human serum mannan-binding protein.
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.
Ma
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Y
Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Yokota
Y
Y
Kozutsumi
Y
Y
Kawasaki
T
T
D000818:Animals; D001704:Biopolymers; D002352:Carrier Proteins / Q000097:blood / Q000737:chemistry* / Q000378:metabolism; D002460:Cell Line; D037222:Collectins; D003167:Complement Activation; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D018411:Spodoptera
D001704:Biopolymers; D002352:Carrier Proteins; D037222:Collectins; D011994:Recombinant Proteins