ArticleInfection and immunity1999
Identification of an intestinal neutral glycosphingolipid as a phenotype-specific receptor for the K88ad fimbrial adhesin of Escherichia coli.
Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 43 citations in OpenAlex.
- Beyond FimH: Diversity and Relevance of Carbohydrate-Binding Fimbrial Proteins in Escherichia coli.Chembiochem : a European journal of chemical biology · 2025Review
- Resistance to ETEC F4/F18-mediated piglet diarrhoea: opening the gene black box.Tropical animal health and production · 2019Review
- Methodology and application ofJournal of animal science and biotechnology · 2019Review
- Intestinal challenge with enterotoxigenicAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2017Review
- Animal Enterotoxigenic Escherichia coli.EcoSal Plus · 2016Review
- Porcine aminopeptidase N binds to F4+ enterotoxigenic Escherichia coli fimbriae.Veterinary research · 2016Article
- Structural and functional insight into the carbohydrate receptor binding of F4 fimbriae-producing enterotoxigenic Escherichia coli.The Journal of biological chemistry · 2015Article
- F4-related mutation and expression analysis of the aminopeptidase N gene in pigs.Journal of animal science · 2014Article
- Refined candidate region for F4ab/ac enterotoxigenic Escherichia coli susceptibility situated proximal to MUC13 in pigs.PloS one · 2014Article
- The search for the gene mutations underlying enterotoxigenic Escherichia coli F4ab/ac susceptibility in pigs: a review.Veterinary research · 2012Review
- Erythrocyte and porcine intestinal glycosphingolipids recognized by F4 fimbriae of enterotoxigenic Escherichia coli.PloS one · 2011Article
- Recognition of blood group ABH type 1 determinants by the FedF adhesin of F18-fimbriated Escherichia coli.The Journal of biological chemistry · 2009Article
- Characterization of the binding specificity of K88ac and K88ad fimbriae of enterotoxigenic Escherichia coli by constructing K88ac/K88ad chimeric FaeG major subunits.Infection and immunity · 2009Article
- Expression of putative Escherichia coli heat-labile enterotoxin (LT) receptors on intestinal brush borders from pigs of different ages.Veterinary research communications · 2006Article
- Evaluation of receptor binding specificity of Escherichia coli K88 (F4) fimbrial adhesin variants using porcine serum transferrin and glycosphingolipids as model receptors.Infection and immunity · 2002Article
- Inhibition of adhesion of Escherichia coli k88ac fimbria to its receptor, intestinal mucin-type glycoproteins, by a monoclonal antibody directed against a variable domain of the fimbria.Infection and immunity · 2000Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In this study, we identified a receptor for the K88ad fimbrial adhesin of Escherichia coli in neutral glycosphingolipid preparations from intestinal epithelial cells of K88ad-adhesive pigs, which was absent in preparations from K88ad-nonadhesive pigs. Neither K88ab nor K88ac adhesin variants bound to this neutral glycosphingolipid. Because this receptor is an intestinal glycosphingolipid that binds K88ad adhesin, it has been designated IGLad. Carbohydrate compositional analysis of a partially purified preparation of IGLad identified galactose, glucose, and N-acetylglucosamine in a ratio of 1.5:1.0:0.5 as the major monosaccharides. Preliminary characterization experiments using lectins showed that IGLad contains the terminal glycanic structure Galbeta1-4GlcNAc. Removal of terminal beta-linked galactose residues from IGLad decreased the recognition of IGLad by the K88ad adhesin, indicating that terminal beta-linked galactose is an essential component of the K88ad adhesin recognition site on IGLad. Studies with purified glycosphingolipid standards demonstrated that K88ad adhesin binds to neolactotetraosylceramide (nLc4Cer) (Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glcbeta1-1Cer) , lactotriosylceramide (GlcNAcbeta1-3Galbeta1-4Glcbeta1-1Cer) and lactotetraosylceramide (Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glcbeta1-1Cer) . Based on these studies, IGLad appears to be nLc4Cer.
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Registered trials
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