Two additional bacteriophage-associated glycan hydrolases cleaving ketosidic bonds of 3-deoxy-D- manno-octulosonic acid in capsular polysaccharides of Escherichia coli

• Published in: FEBS letters 1987-08, Vol.221 (1), p.145-149
• Main Authors: Altmann, Friedrich, März, Leopold, Stirm, Stephan, Unger, Frank M.
• Format: Article
• Language: English
• Subjects: 3-Deoxy-D- manno-2-octulosonic acid; 3-deoxy-D-manno-octulosonic acid; Antigens, Bacterial - metabolism; Antigens, Surface - metabolism; Bacteriophage; Bacteriophages - enzymology; Bacteriophages - ultrastructure; Biological and medical sciences; Capsular polysaccharide; capsules; Escherichia coli; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Glycan hydrolase; Glycoside Hydrolases - metabolism; KDO; Microbiology; Microscopy, Electron; pfu; phages; plaque-forming units: TBA, 2-thiobarbituric acid; polysaccharides; Polysaccharides, Bacterial - metabolism; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Substrate Specificity; Sugar Acids - metabolism; Virology
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(87)80369-1

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.