Leece, R. and Hirst, T.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 available from this repository. (Contact us about this Publication)|
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.
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:||31 Aug 2009 16:45|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/22341 (The current URI for this page, for reference purposes)|
- Depositors only (login required):