Expression of the B-Subunit of Escherichia-Coli Heat-Labile Enterotoxin in a Marine Vibrio and In a Mutant That Is Pleiotropically Defective In the Secretion of Extracellular Proteins

Leece, Robin and Hirst, Timothy R. (1992) Expression of the B-Subunit of Escherichia-Coli Heat-Labile Enterotoxin in a Marine Vibrio and In a Mutant That Is Pleiotropically Defective In the Secretion of Extracellular Proteins. Journal of General Microbiology, 138 . pp. 719-724. ISSN 0022-1287. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1099/00221287-138-4-719

Abstract

A marine Vibrio (designated Vibrio sp. 60) that is related to Vibrio anguillarum was used as a host for a plasmid that encodes the non-toxic B subunit (EtxB) of Escherichia coli heat-labile enterotoxin. Expression of EtxB in Vibrio sp. 60 resulted in the efficient and selective secretion of the B subunit into the extracellular growth medium. This indicated that Vibrio sp. 60, which does not normally produce cholera-like enterotoxins, nonetheless possesses a secretory machinery that permits these toxins to be translocated across its cytoplasmic and outer membranes. Expression of EtxB in a sec mutant of Vibrio sp. 60 (MVT1192), which had previously been shown to be defective in the secretion of several extracellular proteins, resulted in approximately 95% of the B subunit remaining entrapped within the periplasm of the bacterial cell envelope. This implies that the mutation in MVT1192 defines a locus that determines a common step in the secretion of extracellular proteins, including oligomeric toxins.

Item Type: Article
Subjects: Q Science
Q Science > QR Microbiology
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: M. Nasiriavanaki
Date Deposited: 31 Aug 2009 16:45
Last Modified: 19 Jun 2014 15:24
Resource URI: https://kar.kent.ac.uk/id/eprint/22341 (The current URI for this page, for reference purposes)
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