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J Biol Chem, Vol. 273, Issue 33, 20721-20727, August 14, 1998
From the The Hakata antigen is a novel, thermolabile
Cloning and Characterization of the Hakata Antigen, a Member
of the Ficolin/Opsonin p35 Lectin Family
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Department of Clinical Chemistry and
Laboratory Medicine, and the ¶ Department of Anatomy, Faculty of
Medicine, Kyushu University 3-1-1, Maidashi, Higashi-ku, Fukuoka
812-8582, Japan
2-macroglycoprotein that reacts with sera from
patients suffering from systemic lupus erythematosus. In this study we
present the structure and the function of the Hakata antigen. We have
identified cDNA clones encoding the Hakata antigen and analyzed its
function. The cDNA included a possible open reading frame of 897 nucleotides, encoding 299 amino acids. The Hakata antigen consisted of
a collagen-like domain in the middle section and a fibrinogen-like
domain in the COOH terminus, both of which are homologous to human
ficolin-1 and opsonin P35, indicating that these three molecules form a distinct family. The molecular mass of the Hakata antigen expressed in
transfected cells was 35 kDa under reduced conditions, and it formed
ladder bands under nonreducing conditions compatible with the previous
result that the Hakata antigen exists in serum as homopolymers.
Purified Hakata antigen sustained lectin activity, showing affinity
with GalNAc, GlcNAc, D-fucose as mono/oligosaccharide, and
lipopolysaccharides from Salmonella typhimurium and
Salmonella minnesota. These results suggest that the Hakata
antigen, a new member of the ficolin/opsonin P35 family, plays a role
in the serum exerting lectin activity under physiological
conditions.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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