Nucleotide sequence analysis and comparison of the structural genes for Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from Escherichia coli 933

The nucleotide sequence of the Shiga-like toxin type II (SLT-II) structural genes cloned from bacteriophage 933W of the enterohemorrhagic Escherichia coli O157:H7 strain 933 was determined. This sequence was compared with the published sequence for the structural genes of the antigenically distinct Shiga-like toxin type I (SLT-I) encoded by bacteriophage 933J. The SLT-I and SLT-II structural genes shared 58% overall nucleotide and 56% amino acid sequence homologies. The A and B subunits of SLT-I and SLT-II were nearly identical in size and had similar secondary structures and hydropathy plots. The regulation proposed for the SLT-II operon is similar to that previously proposed for SLT-I.

[1]  T. Gojobori,et al.  Evolutionary origin of pathogenic determinants in enterotoxigenic Escherichia coli and Vibrio cholerae O1 , 1987, Journal of bacteriology.

[2]  M. P. Jackson,et al.  Nucleotide sequence analysis of the structural genes for Shiga-like toxin I encoded by bacteriophage 933J from Escherichia coli. , 1987, Microbial pathogenesis.

[3]  N. Seidah,et al.  Complete amino acid sequence of Shigella toxin B-chain. A novel polypeptide containing 69 amino acids and one disulfide bridge. , 1986, The Journal of biological chemistry.

[4]  J. Wells,et al.  Production of Shiga-like toxin by Escherichia coli. , 1986, The Journal of infectious diseases.

[5]  R. Holmes,et al.  Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities , 1986, Infection and immunity.

[6]  J. Friesen,et al.  Cloning and expression of the genes specifying Shiga-like toxin production in Escherichia coli H19 , 1986, Journal of bacteriology.

[7]  B. Rowe,et al.  Cloning of genes determining the production of vero cytotoxin by Escherichia coli. , 1985, Journal of general microbiology.

[8]  B. Rowe,et al.  TWO DISTINCT TOXINS ACTIVE ON VERO CELLS FROM ESCHERICHIA COLI 0157 , 1985, The Lancet.

[9]  R. Holmes,et al.  Cloning of Shiga-like toxin structural genes from a toxin converting phage of Escherichia coli. , 1985, Science.

[10]  D. Thorley-Lawson,et al.  Pathogenesis of Shigella diarrhea. IX. Simplified high yield purification of Shigella toxin and characterization of subunit composition and function by the use of subunit-specific monoclonal and polyclonal antibodies , 1984, The Journal of experimental medicine.

[11]  R. Holmes,et al.  Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea. , 1984, Science.

[12]  J. Mekalanos,et al.  Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development , 1983, Nature.

[13]  H. Smith,et al.  Vero cell toxins in Escherichia coli and related bacteria: transfer by phage and conjugation and toxic action in laboratory animals, chickens and pigs. , 1983, Journal of general microbiology.

[14]  S. Gorbach,et al.  PURIFICATION OF SHIGELLA DYSENTERIAE 1 (SHIGA)-LIKE TOXIN FROM ESCHERICHIA COLI 0157:H7 STRAIN ASSOCIATED WITH HAEMORRHAGIC COLITIS , 1983, The Lancet.

[15]  B. Rowe,et al.  VERO CYTOTOXIN PRODUCTION IN STRAIN OF ESCHERICHIA COLI IS DETERMINED BY GENES CARRIED ON BACTERIOPHAGE , 1983, The Lancet.

[16]  G. Hong,et al.  Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[17]  A. O’Brien,et al.  Purification and characterization of a Shigella dysenteriae 1-like toxin produced by Escherichia coli , 1983, Infection and immunity.

[18]  S. Formal,et al.  ESCHERICHIA COLI 0157:H7 STRAINS ASSOCIATED WITH HAEMORRHAGIC COLITIS IN THE UNITED STATES PRODUCE A SHIGELLA DYSENTERIAE 1 (SHIGA) LIKE CYTOTOXIN , 1983, The Lancet.

[19]  M. Thompson,et al.  Production of Shigella dysenteriae type 1-like cytotoxin by Escherichia coli. , 1982, The Journal of infectious diseases.

[20]  W. Fiers,et al.  Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. , 1982, Gene.

[21]  R. Doolittle,et al.  A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.

[22]  F. Sanger,et al.  Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. , 1980, Journal of molecular biology.

[23]  C. Yanofsky,et al.  Translational coupling during expression of the tryptophan operon of Escherichia coli. , 1980, Genetics.

[24]  S. Osawa,et al.  Evolution of ribosomal proteins in Enterobacteriaceae , 1978, Journal of bacteriology.

[25]  F. Sanger,et al.  DNA sequencing with chain-terminating inhibitors. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[26]  J. Shine,et al.  The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[27]  D. Oliver.  Protein secretion in Escherichia coli. , 1985, Annual review of microbiology.

[28]  D Court,et al.  Regulatory sequences involved in the promotion and termination of RNA transcription. , 1979, Annual review of genetics.