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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 1
Author(s) -
Koizumi Nobuo,
Imamura Morikazu,
Kadotani Tomoyuki,
Yaoi Katsuro,
Iwahana Hidenori,
Sato Ryoichi
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01701-3
Subject(s) - bombyx mori , c type lectin , hemolymph , lectin , bombyx , biochemistry , complementary dna , biology , peptide sequence , cloning (programming) , lipid a , lipopolysaccharide , microbiology and biotechnology , gene , immunology , computer science , programming language
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.