Structure and function of a novel coliphage-associated sialidase

FEMS Microbiol Lett. 2000 Jan 15;182(2):333-7. doi: 10.1111/j.1574-6968.2000.tb08917.x.

Abstract

A coliphage named 63D, isolated previously, associated sialidase as a component of phage particles. In order to localize the enzyme in phage particles, phages were partially destroyed by sonication, and the disrupted particles were size fractionated using a sucrose density gradient. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, enzyme assay and electron micrography of the fractions revealed the enzyme to be composed of four identical subunits with a molecular mass of 90 kDa, and the subunits were cross-linked by disulfide bonds. Electron micrographic observation indicated that six enzyme molecules were localized in a phage tail plate as a hexagonal array.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Fractionation
  • Coliphages / enzymology*
  • Coliphages / physiology
  • Coliphages / ultrastructure
  • Disulfides / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / virology
  • Microscopy, Immunoelectron
  • Neuraminidase / chemistry*
  • Neuraminidase / metabolism*

Substances

  • Disulfides
  • Neuraminidase