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Structural and functional roles of the amino‐terminal region and collagen‐like domain of human serum mannan‐binding protein
Author(s) -
Ma Yong,
Yokota Yasunori,
Kozutsumi Yasunori,
Kawasaki Toshisuke
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201593
Subject(s) - collectin , mannan binding lectin , sf9 , recombinant dna , mannan , lectin , complement system , biochemistry , c type lectin , complementary dna , biology , microbiology and biotechnology , chemistry , immune system , immunology , receptor , gene , polysaccharide , innate immune system , spodoptera
The serum mannan‐binding protein (S‐MBP) is a Ca2+‐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.