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Two additional bacteriophage‐associated glycan hydrolases cleaving ketosidic bonds of 3‐deoxy‐D‐ manno ‐octulosonic acid in capsular polysaccharides of Escherichia coli
Author(s) -
Altmann Friedrich,
März Leopold,
Stirm Stephan,
Unger Frank M.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80369-1
Subject(s) - escherichia coli , glycan , bacteriophage , polysaccharide , biochemistry , enzyme , chemistry , hydrolase , hydrolysis , glycoside hydrolase , biology , microbiology and biotechnology , gene , glycoprotein
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.