Production of a non-toxic site-directed mutant of Clostridium perfringens ε-toxin which induces protective immunity in mice

References

1. Bhown A. S., Habeeb A. F. S. A. 1977; Structural studies on ε- prototoxin of Clostridium perfingens type D. Localisation of the site of tryptic scission necessary for activation to ε-toxin.. Biochem Biophys Res Commun 73:889–896
   [Google Scholar]
2. Bordo D., Argos P. 1991; Suggestions for ‘safe’ residue substitutions in site-directed mutagenesis.. J Mol Biol 217:721–729
   [Google Scholar]
3. Brooks M. E., Sterne M., Warrack G. H. 1957; A reassessment of the criteria used for type differentiation of Clostridium perfringens . J Pathol Bacteriol 74:185–195
   [Google Scholar]
4. Bullen J. J. 1970 Role of toxins in host-parasite relationships.. In Microbial Toxins vol 1 pp 233–276 Edited by Ajl S., Kadis S., Montie T. C. New York: Academic Press;
   [Google Scholar]
5. Bullen J. J., Batty I. 1956; The effect of Clostridium welcbii type D culture filtrates on the permeability of the mouse intestine.. J Pathol Bacteriol 71:311–323
   [Google Scholar]
6. Bullen J. J., Scarisbrick R. 1957; Enterotoxaemia of sheep: experimental reproduction of the disease.. J Pathol Bacteriol 73:494–509
   [Google Scholar]
7. Buxton A., Fraser G. 1977 Animal Microbiology vol 1 pp 205–228 Oxford Blackwell Scientific Publications:
   [Google Scholar]
8. Canard B., Saint Joanis B., Cole S. T. 1992; Genomic diversity and organization of virulence genes in the pathogenic anaerobe Clostridium perfringens . Mol Microbiol 6:1421–1429
   [Google Scholar]
9. Chou P. Y., Fasman G. D. 1978; Prediction of the secondary structure of proteins from their amino acid sequence.. Adv Enzymol 47:45–148
   [Google Scholar]
10. Garnier J., Osguthorpe D., Robson B. 1978; Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins.. J Mol Biol 120:97–120
    [Google Scholar]
11. Habeeb A. F. 1969; Studies on epsilon-prototoxin of Clostridium perfringens type D. I. Purification methods: evidence for multiple forms of epsilon-prototoxin.. Arch Biochem Biophys 130:430–440
    [Google Scholar]
12. Havard H. L., Hunter S. E., Titball R. W. 1992; Comparison of the nucleotide sequence and development of a PCR test for the epsilon toxin gene of Clostridium perfringens type B and type D.. FEMS Microbiol Lett 76:77–81
    [Google Scholar]
13. Hunter S. E., Clarke I. N., Kelly D. C., Titball R. W. 1992; Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coli . Infect Immun 60:102–110
    [Google Scholar]
14. Logan A. J., Williamson E. D., Titball R. W., Percival D. A., Shuttleworth A. D., Conlan J. W., Kelly D. C. 1991; Epitope mapping of the alpha-toxin of Clostridium perfringens . Infect Immun 59:4338–4342
    [Google Scholar]
15. Marmur J. 1961; A procedure for the isolation of deoxyribonucleic acid from micro-organisms.. J Mol Biol 3:208–218
    [Google Scholar]
16. Nakamaye K. L., Eckstein F. 1986; Inhibition of restriction endonuclease Neil cleavage by phosphorothioate groups and its application to oligonucleotide-directed mutagenesis.. Nucleic Acids Res 14:9679–9698
    [Google Scholar]
17. Payne D. W., Williamson E. D., Havard H., Modi N., Brown J. 1994; Evaluation of a new cytotoxicity assay for Clostridium perfringens type D epsilon toxin.. FEMS Microbiol Lett 116:161–167
    [Google Scholar]
18. Percival D. A., Shuttleworth A. D., Williamson E. D., Kelly D. C. 1990; Anti-idiotypic antibody-induced protection against Clostridium perfringens type D.. Infect Immun 58:2487–2492
    [Google Scholar]
19. Sakurai J., Nagahama M. 1985; Role of one tryptophan residue in the lethal activity of Clostridium perfringens epsilon toxin.. Biochem Biophys Res Commun 128:760–766
    [Google Scholar]
20. Sakurai J., Nagahama M. 1986; Amino groups in Clostridium perfringens epsilon prototoxin and epsilon toxin.. Microb Pathog 1:417–423
    [Google Scholar]
21. Sakurai J., Nagahama M. 1987a; Histidine residues in Clostridium perfringens epsilon toxin.. FEMS Microbiol Lett 41:317–319
    [Google Scholar]
22. Sakurai J., Nagahama M. 1987b; The inactivation of Clostridium perfringens epsilon toxin by treatment with tetra- nitromethane and N-acetylimidazole.. Toxicon 25:279–284
    [Google Scholar]
23. Sakurai J., Nagahama M. 1987c; Carboxyl groups in Clostridium perfringens epsilon toxin.. Microb Pathog 3:469–474
    [Google Scholar]
24. Sambrook J., Fritsch E. F., Maniatis T. 1989 MolecularCloning: a Laboratory Manual 2nd edn Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
25. Sayers J. R., Schmidt W., Eckstein F. 1988; 5ʹ-3ʹ exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis.. Nucleic Acids Res 16:791–801
    [Google Scholar]
26. Smith L. D., Williams B. L. 1984 The Pathogenic Anaerobic Bacteria 3rd edn Springfield, Illinois: Charles C. Thomas;
    [Google Scholar]
27. Stephen J., Pietrowski R. A. 1986 Bacterial Toxins 2nd edn Wokingham, England: van Nostrand Reinhold (UK);
    [Google Scholar]
28. Stokka G. L., Edwards A. J., Spire M. F., Brandt R. T., Smith J. E. 1994; Inflammatory response to clostridial vaccines in feedlot cattle.. J Am Vet Med Assoc 204:415–419
    [Google Scholar]
29. Taylor J. W., Ott J., Eckstein F. 1985a; The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA.. Nucleic Acids Res 13:8765–8785
    [Google Scholar]
30. Taylor J. W., Schmidt W., Cosstick R., Okruszek A., Eckstein E. 1985b; The use of phosphorothioate-modified DNA in restriction enzyme reactions to prepare nicked DNA.. Nucleic Acids Res 13:8749–8764
    [Google Scholar]
31. Thanabalu T., Porter A. G. 1996; A Bacillus sphaericus gene encoding a novel type of mosquitocidal toxin of 38 kDa.. Gene 170:85–89
    [Google Scholar]
32. Titball R. W., Hunter S. E., Martin K. L., Morris B. C., Shuttle- worth A. D., Rubidge T., Anderson D. W., Kelly D. C. 1989; Molecular cloning and nucleotide sequence of the alpha-toxin (phospholipase) of Clostridium perfringens . Infect Immun 57:367–376
    [Google Scholar]
33. Worthington R. W., Mulders M. S. 1977; Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation.. Infect Immun 18:549–551
    [Google Scholar]
34. Worthington R. W., Mulders M. S., van Rensburg J. J. 1973; Enzymatic activation of Clostridium perfringens epsilon prototoxin and some biological properties of activated toxin.. Onder- stepoort J Vet Res 40:151–154
    [Google Scholar]