The Shiga-toxin VT2-encoding bacteriophage varphi297 integrates at a distinct position in the Escherichia coli genome

Biochim Biophys Acta. 2002 Dec 12;1579(2-3):196-202. doi: 10.1016/s0167-4781(02)00539-0.

Abstract

The plaque-forming VT2-encoding lambdoid bacteriophage varphi297 was isolated from a Belgian clinical Escherichia coli O157:H7 isolate. PCR walking, starting from the int gene of phage varphi297, demonstrated that the varphi297 prophage integrated in the yecE gene of a lysogenic E. coli K12 strain. This integration site, in E. coli K12 and in the original clinical O157:H7 isolate, was confirmed by PCR using primers flanking this site. The excisionase protein of phage varphi297 is identical to the excisionase of VT1-encoding phage VT1-Sakai, while the integrases, which are 82% identical, show significant sequence divergence in the central and C-terminal region. This can explain the different integration sites of both prophages. The activity of the integrase was proven by its ability to mediate the integration of a suicide plasmid, carrying the attachment site of varphi297, at the appropriate position in the E. coli chromosome.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriophages / genetics*
  • Base Sequence
  • Binding Sites
  • DNA Nucleotidyltransferases / genetics
  • Escherichia coli O157 / genetics*
  • Escherichia coli O157 / isolation & purification
  • Escherichia coli O157 / virology
  • Evolution, Molecular
  • Humans
  • Integrases / genetics
  • Lysogeny
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Prophages / genetics
  • Sequence Alignment
  • Shiga Toxin 2 / chemistry
  • Shiga Toxin 2 / genetics*
  • Viral Proteins*
  • Virus Integration

Substances

  • Shiga Toxin 2
  • Viral Proteins
  • DNA Nucleotidyltransferases
  • Integrases
  • excisionase