A caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection

Hiroko Ideo, Keiko Fukushima, Keiko Genyo-Ando, Shohei Mitani, Katsufumi Dejima, Kazuya Nomura, Katsuko Yamashita

Research output: Contribution to journalArticle

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Abstract

Galectins are a family of β-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.Wefound 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.

Original languageEnglish
Pages (from-to)26493-26501
Number of pages9
JournalJournal of Biological Chemistry
Volume284
Issue number39
DOIs
Publication statusPublished - Sep 25 2009

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Galectins
Glycolipids
Caenorhabditis elegans
Bacterial Infections
Galectin 1
Biological Phenomena
Galactosides
Bacillus thuringiensis
Competitive Binding
Molecules
Biosynthesis
Lectins
Bacilli
Intestines
Carrier Proteins
Escherichia coli
Carbohydrates
Animals
Genes
Mutation

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Ideo, H., Fukushima, K., Genyo-Ando, K., Mitani, S., Dejima, K., Nomura, K., & Yamashita, K. (2009). A caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection. Journal of Biological Chemistry, 284(39), 26493-26501. https://doi.org/10.1074/jbc.M109.038257

A caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection. / Ideo, Hiroko; Fukushima, Keiko; Genyo-Ando, Keiko; Mitani, Shohei; Dejima, Katsufumi; Nomura, Kazuya; Yamashita, Katsuko.

In: Journal of Biological Chemistry, Vol. 284, No. 39, 25.09.2009, p. 26493-26501.

Research output: Contribution to journalArticle

Ideo, H, Fukushima, K, Genyo-Ando, K, Mitani, S, Dejima, K, Nomura, K & Yamashita, K 2009, 'A caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection', Journal of Biological Chemistry, vol. 284, no. 39, pp. 26493-26501. https://doi.org/10.1074/jbc.M109.038257
Ideo, Hiroko ; Fukushima, Keiko ; Genyo-Ando, Keiko ; Mitani, Shohei ; Dejima, Katsufumi ; Nomura, Kazuya ; Yamashita, Katsuko. / A caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection. In: Journal of Biological Chemistry. 2009 ; Vol. 284, No. 39. pp. 26493-26501.
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