Structural studies of the O-antigen polysaccharides of Klebsiella O5 and Escherichia coli O8
Per‐Erik JanssonJörgen LōnngrenGöran WidmalmKarin LeonteinKerstin SlettengrenStefan B. SvensonGöran WrangsellAnne DellPhilip R. Tiller
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Klebsiella
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Escherichia
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Bovine serum albumin
Monosaccharide
Mannose receptor
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Mannan
Antigenicity
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ABSTRACT In order to determine the determinant antigenic group of the mannan of Saccharomyces cerevisiae , a series of inhibition tests were carried out employing oligosaccharides which separated from the acetolyzate and the hydrolyzate of the mannan. Tetraose, Man α1→3 Man α1→2 Man α→2 Man 2 , corresponding to the structure of the longer branching moieties of the mannan showed the strongest inhibition, while the isomer, Man α1→6 Man α1→6 Man, corresponding to the core moiety, produced only one‐tenth the inhibition of the former. This provides evidence that the branching moieties of the mannan play important role in combining with antibody. The fact that the disaccharide, Man α→3, showed significantly stronger inhibition than those of the other disaccharides, Man α1→2 Man and Man α1→6 Man, indicates that the most important part of the determinant group of the mannan is α1→3 linked D‐mannose residue. The antigenic inactivity of the periodate‐oxidized mannan containing unoxidized mannose residues indicates that the presence of 3‐O‐substituted‐D‐mannose residues adjacent to the D‐mannose residues and joined with α1→d2 linkages, are essential to fit the combining site of the antibody.
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In-Silico Comparative Molecular Docking Studies of Mannan and Mannan Sulphate with Mannose Receptor Abstract The design of nanoparticles for macrophages targeted delivery is based upon selection of most specific carbohydrate polymers. The expression of mannose receptor contributes the selective delivery of nanoparticles to macrophages with high specificity and selectivity. The mannose receptor plays a pivotal role through strong binding of sulphated polysaccharides with cysteine-rich (Cys-Rich) domain. In an effort to search novel carbohydrate polymer for macrophage targeted drug delivery this study aims to evaluate the interaction of mannan sulphate with mannose receptor by computational molecular docking studies. Comparative docking studies were performed for mannan and mannan sulphate, isolated commercially from the cell wall of baker’s yeast (Saccharomyces cerevisiae) with 1DQO mannose protein by Auto Dock software. Molecular docking studies of mannan sulphate with 1DQO mannose protein exhibited strong binding interactions. The results indicated that the docking score of mannan and mannan sulphate with 1DQO protein were found to be -4.114 and -7.185 respectively. This molecular docking analysis could contribute to the further development of nanoparticles synthesis, which may aid in targeting drugs to specific parts of human body containing macrophages. This study concludes that mannan sulphate with interesting biological and structural properties may serve as valuable lead for nanoparticles synthesis for the treatment of human ailments in close proximity to future.
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Mannose receptor
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In a previous study, we reported the excess production of α-1,3-linked mannose residues with the complete disappearance of β-1,2-linked mannose residues in cell wall mannans of Candida albicans serotype A strain cells, which were grown in yeast extract-Sabouraud liquid medium at pH 2.0. In the present study, we examined the immunochemical reactivity of the same mannan of NIH A-207 with an enzyme-linked immunosorbent assay (ELISA) using several antisera to antigenic factors of the genus Candida (FAbs) and the structure of the mannan by two-dimensional homonuclear Hartmann-Hahn analysis. The ELISA showed that the mannan reacts to FAb 4 but not to FAbs 13b and 34, which are reported to be antibody factors against linear side chains containing an α-1,3-linked mannose residue. In the Hartmann-Hahn analysis, we found two branched side chains, Manα1–2Manα1–3[Manα1–6]Manα1-(2Manα1-)22Man and Manα1–3[Manα1–6]Manα1-(2Manα1-)22Man, instead of the previously reported linear side chains. The branched side chains are oversynthesized under acidic conditions.
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SUMMARY: Preparations of flocculent and of non-flocculent cell walls were obtained from flocculent and non-flocculent cells of a strain of Saccharomyces cerevisiae. Flocculent walls contained 46% glucan, 43% mannan, 0.4% P, 1.1% hexosamine, 0.79% non-hexosamine N; non-flocculent walls contained 47% glucan, 44% mannan, 0.3% P, 1.2% hexosamine and 0.98%non-hexosamine N. Mannose-6-phosphate was identified as the principal phosphorus compound present. The mannose residue formed part of the cell-wall mannan and the phosphate was also linked by a second, labile, ester bond to an unidentified site. The degree of phosphorylation of the mannan varied from 1 phosphate to 19 mannose residues in non-flocculent cells to 1 phosphate to 13 residues in flocculent cells.
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The structure of the cell-wall mannan from the J-1012 (serotype A) strain of the polymorphic yeast Candida albicans was determined by acetolysis under mild conditions followed by HPLC and sequential NMR experiments. The serotype A mannan contained beta-1,2-linked mannose residues attached to alpha-1,3-linked mannose residues and alpha-1,6-linked branching mannose residues. Using a beta-1,2-mannosyltransferase, we synthesized a three-beta-1,2-linkage-containing mannoheptaose and used it as a reference oligosaccharide for 1H-NMR assignment. On the basis of the results obtained, we derived an additivity rule for the 1H-NMR chemical shifts of the beta-1,2-linked mannose residues. The morphological transformation of Candida cells from the yeast form to the hyphal form induced a significant decrease in the phosphodiesterified acid-labile beta-1,2-linked manno-oligosaccharides, whereas the amount of acid-stable beta-1,2 linkage-containing side chains did not change. These results suggest that the Candida mannan in candidiasis patients contains beta-1,2-linked mannose residues and that they behave as a target of the immune system.
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Mannan
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Mannosidase
Nuclear Overhauser effect
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Mannan
Monosaccharide
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Bovine serum albumin
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