Purification and characterization of a phage-encoded cytotoxin from an Escherichia coli O111 strain associated with hemolytic-uremic syndrome.

Cytotoxin production by Escherichia coli O111:H-strain HUS-2 (Hamburg) is associated with a temperate toxin-converting bacteriophage (Tcp-111). E. coli laboratory strain C600 transduced and subsequently lysed by the phage produced and liberated large amounts of cytotoxin (CT111) which was purified by sequential chromatography. When compared with published procedures for toxin release from viable cells, lysis of the C600 culture by the phage was most effective. By SDS-PAGE CT111 as Shiga toxin from Shigella dysenteriae 1 were shown to consist of two polypeptides of MW 31 kd and 4-5 kd. Both toxins share common antigenic epitopes as revealed by immunoblotting and neutralization studies. With rabbit anti-CT111 toxic activity of only 5 out of 8 clinical E. coli O111 isolates was neutralized suggesting the presence of different cytotoxins in E. coli serogroup O111. Taken together, our data established CT111 as a potent cytotoxin with significant enterotoxic and neurotoxic properties similar or identical to Shiga toxin and to Shiga-like toxin I from E. coli O26:H11 and O157:H7 strains.