論文

査読有り
2009年9月

A Caenorhabditis elegans Glycolipid-binding Galectin Functions in Host Defense against Bacterial Infection

JOURNAL OF BIOLOGICAL CHEMISTRY
  • Hiroko Ideo
  • ,
  • Keiko Fukushima
  • ,
  • Keiko Gengyo-Ando
  • ,
  • Shohei Mitani
  • ,
  • Katsufumi Dejima
  • ,
  • Kazuya Nomura
  • ,
  • Katsuko Yamashita

284
39
開始ページ
26493
終了ページ
26501
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M109.038257
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

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.

リンク情報
DOI
https://doi.org/10.1074/jbc.M109.038257
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/19635802
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000269969600030&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M109.038257
  • ISSN : 0021-9258
  • eISSN : 1083-351X
  • PubMed ID : 19635802
  • Web of Science ID : WOS:000269969600030

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