The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains.
We recently isolated and characterized the lipopolysaccharide (LPS)-binding protein, BmLBP, from the larval hemolymph of the silkworm Bombyx mori. BmLBP is a pattern recognition molecule that recognizes the lipid A portion of LPS and participates in a cellular defense reaction. This paper describes the cDNA cloning of BmLBP. The deduced amino acid sequence of BmLBP revealed that BmLBP is a novel member of the C-type lectin superfamily with a unique structural feature that consists of two different carbohydrate-recognition domains in tandem, a short and a long form.
Koizumi
N
N
Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan.
Imamura
M
M
Kadotani
T
T
Yaoi
K
K
Iwahana
H
H
Sato
R
R
D000209:Acute-Phase Proteins; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015139:Blotting, Southern; D012831:Bombyx; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D003001:Cloning, Molecular; D018076:DNA, Complementary; D005786:Gene Expression Regulation; D006434:Hemocytes / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D000099231:Lipopolysaccharide-Binding Protein