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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1988-11-4
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pubmed:abstractText |
Uropathogenic Escherichia coli strains designated as ONAP, based on their O negative A positive agglutination of human P1 erythrocytes, were shown to prefer the globo-A glycolipid as a receptor structure. The dependence on both the A terminal and the globoseries chain was confirmed by agglutination of human AP1, but not Ap or OP1 erythrocytes and by binding to the globo-A glycolipid on TLC plates. Neither Gal alpha 1----4Gal beta nor the A trisaccharide GalNAc alpha 1----3(Fuc alpha 1----2)Gal beta alone functioned as receptors. The bacteria thus appeared to recognize an epitope resulting from the combination of the terminal and internal structures.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
237
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
123-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3049148-Animals,
pubmed-meshheading:3049148-Bacterial Adhesion,
pubmed-meshheading:3049148-Blood Group Antigens,
pubmed-meshheading:3049148-Carbohydrate Conformation,
pubmed-meshheading:3049148-Carbohydrate Sequence,
pubmed-meshheading:3049148-Dogs,
pubmed-meshheading:3049148-Escherichia coli,
pubmed-meshheading:3049148-Globosides,
pubmed-meshheading:3049148-Glycolipids,
pubmed-meshheading:3049148-Glycosphingolipids,
pubmed-meshheading:3049148-Hemagglutination,
pubmed-meshheading:3049148-Humans,
pubmed-meshheading:3049148-Species Specificity
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pubmed:year |
1988
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pubmed:articleTitle |
Globo-A--a new receptor specificity for attaching Escherichia coli.
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pubmed:affiliation |
Department of Clinical Immunology, University of Göteborg, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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