Linked Life Data

19635802

Source:http://linkedlifedata.com/resource/pubmed/id/19635802

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
2009-9-21
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26493-501
pubmed:dateRevised
2010-9-29
pubmed:meshHeading
pubmed-meshheading:19635802-Animals, pubmed-meshheading:19635802-Bacillus thuringiensis, pubmed-meshheading:19635802-Bacterial Proteins, pubmed-meshheading:19635802-Caenorhabditis elegans, pubmed-meshheading:19635802-Caenorhabditis elegans Proteins, pubmed-meshheading:19635802-Chromatography, High Pressure Liquid, pubmed-meshheading:19635802-Endotoxins, pubmed-meshheading:19635802-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:19635802-Galectins, pubmed-meshheading:19635802-Glycolipids, pubmed-meshheading:19635802-Green Fluorescent Proteins, pubmed-meshheading:19635802-Hemolysin Proteins, pubmed-meshheading:19635802-Host-Pathogen Interactions, pubmed-meshheading:19635802-Intestines, pubmed-meshheading:19635802-Mutation, pubmed-meshheading:19635802-Protein Binding, pubmed-meshheading:19635802-Protein Isoforms, pubmed-meshheading:19635802-Recombinant Proteins
pubmed:year
2009
pubmed:articleTitle
A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection.
pubmed:affiliation
Innovative Research Initiatives, Tokyo Institute of Technology, Yokohama 226-8503, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't