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A novel expression system for Salmonella typhimurium allowing high production levels, product secretion and efficient recovery.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1996 Jan 05; Vol. 218 (1), pp. 356-9. - Publication Year :
- 1996
-
Abstract
- A novel expression system for heterologous production in Salmonella typhimurium, taking advantage of the promoter, signal sequence and two IgG-binding domains (ZZ) from staphylococcal protein A, has been investigated. The production of two different fusion proteins, ZZ-M3 and ZZ-M5, was characterized in terms of production levels, product localization (periplasma or culture medium) and product quality after affinity purification. High expression levels and efficient product secretion were obtained, making the system attractive for vaccine development. The potential use of S. typhimurium as host for heterologous production in biotechnology is discussed.
- Subjects :
- Amino Acid Sequence
Binding Sites
Electrophoresis, Polyacrylamide Gel
Escherichia coli genetics
Genes, Bacterial
Immunoglobulin G metabolism
Molecular Sequence Data
Molecular Weight
Promoter Regions, Genetic
Protein Sorting Signals biosynthesis
Protein Sorting Signals metabolism
Recombinant Fusion Proteins isolation & purification
Salmonella typhimurium genetics
Salmonella typhimurium growth & development
Staphylococcal Protein A isolation & purification
Escherichia coli metabolism
Recombinant Fusion Proteins biosynthesis
Salmonella typhimurium metabolism
Staphylococcal Protein A biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 218
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 8573161
- Full Text :
- https://doi.org/10.1006/bbrc.1996.0062