CONTRACTILE-TAILED BACTERIOPHAGES ADSORB TO ESCHERICHIA-COLI O128AB LIPOPOLYSACCHARIDE THAT IS ALTERED BY LARGE PLASMIDS TO PROVIDE RECEPTORS AND LIPOPOLYSACCHARIDE HETEROGENEITY WITHIN THE SEROGROUP
Ml. Kalmokoff et De. Bradley, CONTRACTILE-TAILED BACTERIOPHAGES ADSORB TO ESCHERICHIA-COLI O128AB LIPOPOLYSACCHARIDE THAT IS ALTERED BY LARGE PLASMIDS TO PROVIDE RECEPTORS AND LIPOPOLYSACCHARIDE HETEROGENEITY WITHIN THE SEROGROUP, Canadian journal of microbiology, 41(2), 1995, pp. 163-169
The verotoxigenic Escherichia coli strain H.I.8 (originally O128:B12,
now not typeable) contained a ColB+M plasmid and two morphologically i
dentical temperate bacteriophages (H18A and H18B). Both phages were O1
28ab specific, using the lipopolysaccharide O side chains of susceptib
le clinical isolates as receptors. SDS polyacrylamide gel electrophore
sis with silver staining of O128ab lipopolysaccharide revealed four di
stinct types of ladder with different interband spacings. No specifici
ty was found between ladder type and sensitivity to either phage. One
of the numerous large plasmids present in O128ab isolates was found to
modify the structure of the lipopolysaccharide O side chains to provi
de phage receptors.