title: 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.
abstract: 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.
authors.affiliation: Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Koizumi
authors.forename: M
authors.initials: M
authors.lastname: Imamura
authors.forename: T
authors.initials: T
authors.lastname: Kadotani
authors.forename: K
authors.initials: K
authors.lastname: Yaoi
authors.forename: H
authors.initials: H
authors.lastname: Iwahana
authors.forename: R
authors.initials: R
authors.lastname: Sato
mesh_terms: 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