Amin, Tehmina and 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. (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)
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.
|Subjects:||Q Science > QP Physiology (Living systems) > QP517 Biochemistry|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||P. Ogbuji|
|Date Deposited:||27 Aug 2009 17:55|
|Last Modified:||13 Jun 2014 13:16|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/20356 (The current URI for this page, for reference purposes)|