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Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins.

Authors
  • Pelkonen, S
  • Pelkonen, J
  • Finne, J
Type
Published Article
Journal
Journal of virology
Publication Date
Oct 01, 1989
Volume
63
Issue
10
Pages
4409–4416
Identifiers
PMID: 2778882
Source
Medline
License
Unknown

Abstract

The cleavage specificities of seven bacteriophage endosialidases degrading the alpha 2-8-linked polysialic acid common to bacterial polysaccharides and to the cell adhesion molecule N-CAM were investigated. The bacteriophages studied represented five different phenotypic groups by protein and DNA fragment analysis and two different morphology groups by electron microscopy. Characterization of the fragments arising from the native or chemically modified substrates of different sizes showed that cleavage specificity was influenced by enzyme concentration. At the initial phase of degradation, at concentrations ranging from 20- to 100-fold, the minimum substrate size was an oligomer of eight (in one case, nine) sialic acid units that was preferably cleaved at the same position. Under exhaustive conditions, the oligomers were degraded further, and each enzyme type had its own specificity. The similar initial cleavage of polysialic acid by endosialidases associated with phages of different properties and morphology suggests a conserved mechanism of enzyme-substrate interaction. This mechanism may be conformationally determined and related to the specific properties of polysialic acid in other molecular interactions.

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