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- Bock, K, et al.
(author)
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Specificity of binding of a strain of uropathogenic Escherichia coli to Gal alpha 1----4Gal-containing glycosphingolipids.
- 1985
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In: The Journal of biological chemistry. - 0021-9258. ; 260:14, s. 8545-51
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Journal article (peer-reviewed)abstract
- A strain of Escherichia coli originally isolated from urine of a patient with acute pyelonephritis was studied in detail for binding to glycosphingolipids. Bacteria labeled metabolically with [14C]glucose were layered over a glycolipid chromatogram and bound bacteria were detected by autoradiography. The detection was down to a few ng of glycolipid (pmol level) under these assay conditions. At a test level of 500 ng all glycolipids (more than a dozen molecular species analyzed) with Gal alpha 1----4Gal as an internal or terminal part bound the bacteria strongly while glycolipids known to lack this sequence were negative. Conformational analysis using hard sphere calculations including the exo-anomeric effect showed a bend in the saccharide chain at this disaccharide with a largely hydrophobic surface of the convex side, probably being part of the binding epitope. Mixtures of glycolipids isolated from a human ureter scraping and from urinary sediments bound bacteria in the 2- to 7-sugar interval. Thus, this infectious strain of E. coli recognizes glycolipids being present in epithelial cells lining the urinary tract.
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| 7. |
- Breimer, Michael, 1951, et al.
(author)
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Structures of the eight- to nine-sugar glycolipids of human blood group A erythrocytes.
- 1988
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In: Carbohydrate research. - 0008-6215. ; 178, s. 111-20
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Journal article (peer-reviewed)abstract
- Two glycolipid fractions, isolated in 1975 from blood group A1 erythrocytes and shown on the basis of direct-inlet mass spectrometry to contain eight- and nine-sugar A-type sequences, have been reinvestigated by fast-atom-bombardment mass spectrometry and overlay analysis with selected monoclonal anti-A antibodies. The presence of three separate glycolipids was concluded, consistent with a common paragloboside backbone [beta-D-Galp-(1----4)-beta-D-GlcpNAc-(1----3)-beta-D-Galp-(1----4)-D-Glc] and a typical erythrocyte ceramide component (sphingosine, and 22-, 23-, 24-, and 25-carbon nonhydroxy fatty acids). It is proposed that they carry A determinants based on Type 1 [beta-D-Galp-(1----3)-beta-D-GlcpNAc], Type 2 [beta-D-Galp-(1----4)-beta-D-GlcpNAc], and Type 3 [beta-D-Galp-(1----3)-alpha-D-GalpNAc] chains, respectively. The Type 1 (eight sugars) and Type 3 (nine sugars) glycolipids appeared in mixtures of both the native and the acetylated form. The existence of Type 1 glycolipid, which appears to be a genuine erythrocyte glycolipid as concluded from the ceramide composition, had been predicted earlier by other workers.
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| 9. |
- Gane, P, et al.
(author)
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Heterogeneity of anti-A and anti-B monoclonal reagents. Agglutination of some weak ABH erythrocyte variants and recognition of synthetic oligosaccharide and tissue antigens.
- 1987
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In: Vox sanguinis. - 0042-9007. ; 53:2, s. 117-25
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Journal article (peer-reviewed)abstract
- Eight anti-A and seven anti-B monoclonal reagents were tested in parallel, with normal and weak ABH red cell phenotypes. A whole range of different reactivity patterns was found, but by making a comparison with the results obtained using polyclonal standard reagents, two major categories of reagents were distinguished: (a) stronger and more specific reagents, and (b) reagents similar to, or weaker than, the standard polyclonal controls. The analysis of the specificity of the reagents by tissue fluorescence staining and reactivity with synthetic oligosaccharides and purified glycolipids confirmed the existence of broad and restricted specificities. Two kinds of anti-A1 reagents are described. One related to type 3/4 structures, which stains the Golgi apparatus, and another with broad anti-A specificity which cross-reacts with 'A-like' structures. The inhibition of anti-A reagents with salivas and synthetic oligosaccharide antigens gave parallel results for the secretor salivas and the difucosylated A antigens.
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