Reversible cross-linking of crystalline bacterial surface layer glycoproteins through their glycan chains |
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Authors: | Paul Messner Max Wellan Wolfgang Kubelka Uwe B. Sleytr |
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Affiliation: | (1) Zentrum für Ultrastrukturforschung und Ludwig-Boltzmann-Institut für Molekulare Nanotechnologie, Universität für Bodenkultur, Gregor-Mendel-Strasse 33, A-1180 Vienna, Austria;(2) Institut für Pharmakognoise, Universität Wien, A-1090 Vienna, Austria |
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Abstract: | After periodate oxidation and incubation with dithiodipropionic acid dihydrazide cross-linking of the crystalline surface layer (S-layer) glycoproteins of Clostridium thermohydrosulfuricum L111-69 and Bacillus alvei CCM 2051 was achieved specifically through the glycan chains. The cross-linked S-layers were used for the immobilization of chemically synthesized, spacer-linked, tumour-associated T-disaccharide [Gal(13)GalNAc]. Electron microscopical evaluation of the resulting conjugates showed densely packed, multilayered S-layer structures loaded with the immobilized ligand. After reductive cleavage of the disulphide bond of dithiodipropionic acid by dithiothreitol, monomeric haptenated S-layer conjugates could be obtained. Both the cross-linked and the monomeric type of conjugate might be useful for assessment of specific immune responses, which, in general, can be elicited by those artificial antigens.Correspondence to: P. Messner |
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