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Dejima Katsufumi
Department School of Medicine, School of Medicine Position Assistant Professor |
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| Article types | Original article |
| Language | English |
| Peer review | Peer reviewed |
| Title | A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection. |
| Journal | Formal name：The Journal of biological chemistry Abbreviation：J Biol Chem ISSN code：1083-351X(Electronic)0021-9258(Linking) |
| Volume, Issue, Page | 284(39),pp.26493-501 |
| Author and coauthor | Ideo Hiroko, Fukushima Keiko, Gengyo-Ando Keiko, Mitani Shohei, Dejima Katsufumi, Nomura Kazuya, Yamashita Katsuko |
| Publication date | 2009/09 |
| Summary | 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 |
| Document No. | 19635802 |