デジマ　カツフミ   Dejima Katsufumi   出嶋　克史    所属   医学部 医学科    職種   助教
論文種別	原著
言語種別	英語
査読の有無	査読あり
表題	A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection.
掲載誌名	正式名：The Journal of biological chemistry 略　 称：J Biol Chem ISSNコード：1083-351X(Electronic)0021-9258(Linking)
巻・号・頁	284(39),pp.26493-501
著者・共著者	Ideo Hiroko, Fukushima Keiko, Gengyo-Ando Keiko, Mitani Shohei, Dejima Katsufumi, Nomura Kazuya, Yamashita Katsuko
発行年月	2009/09
概要	Galectins are a family of beta-galactoside-binding proteins that are widely found among animal species and that regulate diverse biological phenomena. To study the biological function of glycolipid-binding galectins, we purified recombinant Caenorhabditis elegans galectins (LEC-1-11) and studied their binding to C. elegans glycolipids. We found that LEC-8 binds to glycolipids in C. elegans through carbohydrate recognition. It has been reported that Cry5B-producing Bacillus thuringiensis strains can infect C. elegans and that the C. elegans Cry5B receptor molecules are glycolipids. We found that Cry5B and LEC-8 bound to C. elegans glycolipid-coated plates in a dose-dependent manner and that Cry5B binding to glycolipids was inhibited by the addition of LEC-8. LEC-8 is usually expressed strongly in the pharyngeal-intestinal valve and intestinal-rectal valve and is expressed weakly in intestine. However, when C. elegans were fed Escherichia coli expressing Cry5B, intestinal LEC-8::EGFP protein levels increased markedly. In contrast, LEC-8::EGFP expression triggered by Cry5B was reduced in toxin-resistant C. elegans mutants, which had mutations in genes involved in biosynthesis of glycolipids. Moreover, the LEC-8-deficient mutant was more susceptible to Cry5B than wild-type worms. These results suggest that the glycolipid-binding lectin LEC-8 contributes to host defense against bacterial infection by competitive binding to target glycolipid molecules.
DOI	10.1074/jbc.M109.038257
文献番号	19635802