Müller, N; Vogel, M; Gottstein, Bruno; Scholle, A; Seebeck, T (1989). Plasmid vector for overproduction and export of recombinant protein in Escherichia coli: efficient one-step purification of a recombinant antigen from Echinococcus multilocularis (Cestoda). Gene, 75(2), pp. 329-334. Elsevier
Full text not available from this repository. (Request a copy)We describe the use of the Escherichia coli plasmid vector, pVB2, for high-level expression and export of recombinant protein. The pBR322 derivative pVB2 harbors the mglB gene, which codes for the galactose-binding protein (GBP) of E. coli. GBP is exported into the periplasmic space of the bacterial cell. Gene mglB contains an EcoRI restriction site close to its 3' end which allows simple in-frame insertion of EcoRI fragments obtained from recombinant lambda gt11 phages. The pVB2 vector was used to express an antigen from Echinococcus multilocularis. The recombinant protein amounted to over 50% of total cellular protein and could be efficiently isolated from the periplasm by osmotic shock. The application of the purified antigen in an ELISA enabled a clear and specific detection of anti-Ec. multilocularis antibodies in human patients' sera, which had been immunosorbed with a periplasmic extract (containing wt GBP) before investigation. These data show the general usefulness of pVB2 as an expression vector for producing in E. coli diagnostically relevant antigens from any infective organism.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Parasitology |
UniBE Contributor: |
Gottstein, Bruno |
Subjects: |
600 Technology > 630 Agriculture 600 Technology > 610 Medicine & health |
ISSN: |
0378-1119 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Bruno Gottstein |
Date Deposited: |
23 Jul 2018 12:19 |
Last Modified: |
05 Dec 2022 15:16 |
PubMed ID: |
2523840 |
URI: |
https://boris.unibe.ch/id/eprint/118638 |
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