Lipopolysaccharide‐Binding Proteins and their Involvement in the Bacterial Clearance from the Hemolymph of the Silkworm <i>Bombyx Mori</i>

DOI Web Site Web Site 被引用文献5件

抄録

<jats:p>Proteins having the ability to bind to <jats:italic>Escherichia coli</jats:italic> K12W3110 (rough (R) mutant) were isolated and purified by affinity precipitation from the larval hemolymph of the silkworm <jats:italic>Bombyx mori.</jats:italic> These proteins were found to consist of two components with molecular masses of 43 kDa and 40 kDa by SDS/ PAGE. They bound to all <jats:italic>E. coli</jats:italic> R mutants (Ra, Rb<jats:sub>1</jats:sub>, Rc, Rd<jats:sub>1</jats:sub> and Re) and <jats:italic>Salmonella minnesota</jats:italic> R mutants. However, they did not bind to smooth types of the above bacteria. They bound to both lipopolysaccharide(LPS)‐coated and lipid‐A‐coated microtiter plates and have similar dissociation constants for LPS and lipid A. This indicates that the binding proteins recognize the lipid A portion of LPS and thus, we have named these proteins BmLBP (<jats:italic>B. mori</jats:italic> LPS‐binding proteins). We also found that BmLBP participated in the clearance of <jats:italic>E. coli</jats:italic> cells injected into the body cavity of the silkworm.</jats:p>

収録刊行物

被引用文献 (5)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ