PMID: 10620688Jan 6, 2000

Structure and function of a novel coliphage-associated sialidase

FEMS Microbiology Letters
Y MachidaShinji Iijima

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.

Citations

Jan 20, 2004·Journal of Molecular Biology·Dean SchollIan J Molineux
Oct 20, 2005·Journal of Bioscience and Bioengineering·Y MachidaS Iijima
Aug 9, 2005·Applied and Environmental Microbiology·Dean SchollCarl Merril
May 5, 2009·The Journal of Biological Chemistry·Thomas J MorleyStephen G Withers
Jan 12, 2013·Current Protein & Peptide Science·Zuzanna Drulis-KawaRob Lavigne
Mar 25, 2017·Applied Microbiology and Biotechnology·Agnieszka LatkaZuzanna Drulis-Kawa
Jan 31, 2003·The Journal of Biological Chemistry·Martina MühlenhoffRita Gerardy-Schahn

Related Concepts

Cell Fractionation
Coliphages
Disulfides
SDS-PAGE
Alkalescens-Dispar Group
Neuraminidase
Microscopy, Immunoelectron

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