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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1994-9-13
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pubmed:abstractText |
Heat-labile enterotoxins (Etx) are plasmid-encoded, multimeric proteins produced by certain diarrheagenic strains of Escherichia 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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Conditioned,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isopropyl Thiogalactoside,
http://linkedlifedata.com/resource/pubmed/chemical/heat-labile enterotoxin, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1046-5928
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:geneSymbol |
etxB
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
198-204
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pubmed:dateRevised |
2010-8-25
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pubmed:meshHeading |
pubmed-meshheading:8054855-Bacterial Toxins,
pubmed-meshheading:8054855-Chromatography, Liquid,
pubmed-meshheading:8054855-Culture Media, Conditioned,
pubmed-meshheading:8054855-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8054855-Enterotoxins,
pubmed-meshheading:8054855-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:8054855-Escherichia coli,
pubmed-meshheading:8054855-Escherichia coli Proteins,
pubmed-meshheading:8054855-Gene Expression Regulation, Bacterial,
pubmed-meshheading:8054855-Genetic Vectors,
pubmed-meshheading:8054855-Isopropyl Thiogalactoside,
pubmed-meshheading:8054855-Ultrafiltration,
pubmed-meshheading:8054855-Vibrio
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pubmed:year |
1994
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pubmed:articleTitle |
Purification of the B-subunit oligomer of Escherichia coli heat-labile enterotoxin by heterologous expression and secretion in a marine vibrio.
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pubmed:affiliation |
Biological Laboratory, The University, Canterbury, Kent, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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