Skip to main content
NCBI home page
Infection and Immunity logoLink to Infection and Immunity
. 1990 Dec;58(12):4142–4144. doi: 10.1128/iai.58.12.4142-4144.1990

Molecular cloning and nucleotide sequence analysis of cholera toxin genes of the CtxA- Vibrio cholerae strain Texas Star-SR.

T J Brickman 1, M Boesman-Finkelstein 1, R A Finkelstein 1, M A McIntosh 1
PMCID: PMC313787  PMID: 2254034

Abstract

The ctx operons from the Vibrio cholerae El Tor strain 3083 and its CtxA- derivative Texas Star-SR were cloned, and their nucleotide sequences were compared. A single missense mutation in the Texas Star-SR ctxA cistron which results in the substitution of threonine for alanine at position 191 of the 258-amino-acid CtxA precursor was identified. Immunoblot analysis detected the mutant CtxA intracellularly early in the culture cycle but not extracellularly at any growth stage.

Full text

PDF
4142

Images in this article

4143Image
on p.4143

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Finkelstein R. A., Atthasampunna P., Chulasamaya M., Charunmethee P. Pathogenesis of experimental cholera: biologic ativities of purified procholeragen A. J Immunol. 1966 Mar;96(3):440–449. [PubMed] [Google Scholar]
  2. Finkelstein R. A., Fujita K., LoSpalluto J. J. Procholeragenoid: an aggregated intermediate in the formation of choleragenoid. J Immunol. 1971 Oct;107(4):1043–1051. [PubMed] [Google Scholar]
  3. Finkelstein R. A., LoSpalluto J. J. Pathogenesis of experimental cholera. Preparation and isolation of choleragen and choleragenoid. J Exp Med. 1969 Jul 1;130(1):185–202. doi: 10.1084/jem.130.1.185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Finkelstein R. A., Sobocinski P. Z., Atthasampunna P., Charunmethee P. Pathogenesis of experimental cholera: identification of choleragen (procholeragen A) by disc immunoelectrophoresis and its differentiation from cholera mucinase. J Immunol. 1966 Jul;97(1):25–33. [PubMed] [Google Scholar]
  5. Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol. 1978 Mar 25;120(1):97–120. doi: 10.1016/0022-2836(78)90297-8. [DOI] [PubMed] [Google Scholar]
  6. Honda T., Finkelstein R. A. Selection and characteristics of a Vibrio cholerae mutant lacking the A (ADP-ribosylating) portion of the cholera enterotoxin. Proc Natl Acad Sci U S A. 1979 Apr;76(4):2052–2056. doi: 10.1073/pnas.76.4.2052. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  8. Levine M. M., Black R. E., Clements M. L., Lanata C., Sears S., Honda T., Young C. R., Finkelstein R. A. Evaluation in humans of attenuated Vibrio cholerae El Tor Ogawa strain Texas Star-SR as a live oral vaccine. Infect Immun. 1984 Feb;43(2):515–522. doi: 10.1128/iai.43.2.515-522.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Levine M. M., Kaper J. B., Black R. E., Clements M. L. New knowledge on pathogenesis of bacterial enteric infections as applied to vaccine development. Microbiol Rev. 1983 Dec;47(4):510–550. doi: 10.1128/mr.47.4.510-550.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Levine M. M., Kaper J. B., Herrington D., Losonsky G., Morris J. G., Clements M. L., Black R. E., Tall B., Hall R. Volunteer studies of deletion mutants of Vibrio cholerae O1 prepared by recombinant techniques. Infect Immun. 1988 Jan;56(1):161–167. doi: 10.1128/iai.56.1.161-167.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mekalanos J. J., Swartz D. J., Pearson G. D., Harford N., Groyne F., de Wilde M. Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development. Nature. 1983 Dec 8;306(5943):551–557. doi: 10.1038/306551a0. [DOI] [PubMed] [Google Scholar]
  12. Miller V. L., Taylor R. K., Mekalanos J. J. Cholera toxin transcriptional activator toxR is a transmembrane DNA binding protein. Cell. 1987 Jan 30;48(2):271–279. doi: 10.1016/0092-8674(87)90430-2. [DOI] [PubMed] [Google Scholar]
  13. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES