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Science 15 July 1983:
Vol. 221. no. 4607, pp. 289 - 291
DOI: 10.1126/science.6857285

Articles

Science, Vol 221, Issue 4607, 289-291
Copyright © 1983 by American Association for the Advancement of Science


articles

Synthesis and secretion of the plasmid-coded heat-labile enterotoxin of Escherichia coli in Vibrio cholerae

RJ Neill, BE Ivins, and RK Holmes

Both cholera toxin and heat-labile enterotoxin were made and secreted into culture supernatants by Vibrio cholerae containing the enterotoxin plasmid pCG86. Several regulatory mutations in V. cholerae that increased or decreased the synthesis of cholera toxin did not affect production of heat-labile enterotoxin. In contrast, a mutation in V. cholerae that interfered with the secretion of cholera toxin also decreased the secretion of heat-labile enterotoxin, indicating that they are processed by a common secretory pathway. Vibrio cholerae should be useful as a model system for analyzing the secretion of true extracellular proteins by Gram-negative bacteria.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Deletion mutations in N-terminal {alpha}1 helix render heat labile enterotoxin B subunit susceptible to degradation.
P. V. Alone, G. Malik, A. Krishnan, and L. C. Garg (2007)
PNAS 104, 16056-16061
   Abstract »    Full Text »    PDF »
Identification of a protein secretory pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli.
M. Tauschek, R. J. Gorrell, R. A. Strugnell, and R. M. Robins-Browne (2002)
PNAS 99, 7066-7071
   Abstract »    Full Text »    PDF »
A Kinetic Model of Intermediate Formation during Assembly of Cholera Toxin B-subunit Pentamers.
C. Lesieur, M. J. Cliff, R. Carter, R. F. L. James, A. R. Clarke, and T. R. Hirst (2002)
J. Biol. Chem. 277, 16697-16704
   Abstract »    Full Text »    PDF »
In Vivo Expression and Immunoadjuvancy of a Mutant of Heat-Labile Enterotoxin of Escherichia coli in Vaccine and Vector Strains of Vibrio cholerae.
E. T. Ryan, T. I. Crean, M. John, J. R. Butterton, J. D. Clements, and S. B. Calderwood (1999)
Infect. Immun. 67, 1694-1701
   Abstract »    Full Text »    PDF »
Generation of a Monoclonal Antibody That Recognizes the Amino-terminal Decapeptide of the B-subunit of Escherichia coli Heat-labile Enterotoxin.
T. Amin, A. Larkins, R. F. L. James, and T. R. Hirst (1995)
J. Biol. Chem. 270, 20143-20150
   Abstract »    Full Text »    PDF »



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Science. ISSN 0036-8075 (print), 1095-9203 (online)