Amin, Tehmina, Hirst, Timothy R. (1994) Purification of the B-Subunit Oligomer of Escherichia-Coli Heat-Labile Enterotoxin by Heterologous Expression and Secretion in a Marine Virio. Protein Expression and Purification, 5 (2). pp. 198-204. ISSN 1046-5928. (doi:10.1006/prep.1994.1031) (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) (KAR id:20356)
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. | |
Official URL: http://dx.doi.org/10.1006/prep.1994.1031 |
Abstract
Heat-labile enterotoxins (Etx) are plasmid-encoded, multimeric proteins produced by certain diarrheagenic strains of Eschenichia coli. The nontoxic, receptor-binding B subunit (EtxB) of such toxins may be useful as a component of vaccines against enterotoxigenic E. coli, or as a carrier for the delivery of heterologous epitopes to the mucosal immune system. Here we describe a simple method for the purification of EtxB from a marine vibrio harboring a broad-host range controlled expression vector containing the etxB gene. Induction of EtxB resulted in its specific secretion to the medium, to a concentration of greater than 25 mg/liter of culture. The techniques of ultrafiltration and hydrophobic interaction chromatography were used to purify EtxB to homogeneity from the medium of this organism (with a yield of 60.7%). EtxB-epitope fusion proteins were also successfully expressed and secreted in this marine vibrio, suggesting that this system may be of general use in the preparation of EtxB-based vaccines. (C) 1991 Academic Press,Inc.
Item Type: | Article |
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DOI/Identification number: | 10.1006/prep.1994.1031 |
Subjects: | Q Science > QP Physiology (Living systems) > QP517 Biochemistry |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | P. Ogbuji |
Date Deposited: | 27 Aug 2009 17:55 UTC |
Last Modified: | 16 Nov 2021 09:58 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/20356 (The current URI for this page, for reference purposes) |
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