Two additional bacteriophage-associated glycan hydrolases cleaving ketosidic bonds of 3-deoxy-D-manno-octulosonic acid in capsular polysaccharides of Escherichia coli |
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| Authors: | F Altmann L M?rz S Stirm F M Unger |
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| Affiliation: | 1. Institut für Chemie der Universität für Bodenkultur Wien, A-1180 Wien, Austria;2. Biochemisches Institut am Klinikum der Universität, D-6300 Giessen, FRG;3. Sandoz Forschungsinstitut Wien, A-1235 Wien, Austria |
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| Abstract: | Two bacteriophages degrading 3-deoxy-D-manno-2-octulosonic acid-(KDO)-containing capsules of Escherichia coli strains were identified. Using modifications of the thiobarbituric acid assay, it was shown that each phage contains a glycan hydrolase activity cleaving one type of ketosidic linkage of KDO. Thus, the enzyme from phage ψ95 catalyses the hydrolysis of β-octulofuranosidonic linkages of the K95 glycan; and ψ1092, the α-octulopyranosidonic linkages of the K? antigen of E. coli LP1092. No cross-reactivity of the phage enzymes with other KDO-containing capsular polysaccharides was observed. |
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