Secretion of recombinant proteins into the culture medium by Escherichia coli and Staphylococcus aureus.
@article{Uhln1989SecretionOR,
title={Secretion of recombinant proteins into the culture medium by Escherichia coli and Staphylococcus aureus.},
author={M Uhl{\'e}n and Lars Abrahms{\'e}n},
journal={Biochemical Society transactions},
year={1989},
volume={17 2},
pages={
340-1
}
}The ability of staphylococcal protein A (SPA) to bind to the Fc part of IgG has been used for the purification of a number of heterologous gene products as fusion proteins. Both the SPA promoter and signal sequence function in Escherichia coli, as well as in a number of Gram-positive bacteria, which facilitates comparisons of the expressed specific products in different hosts. The expression system developed for E. coli yields excretion of the fusion protein to the growth medium, which makes E…
Tables from this paper
9 Citations
Engineering a novel secretion signal for cross-host recombinant protein expression.
- BiologyProtein engineering
- 2002
The identification of a novel secretion signal (SS) that is capable of directing the secretion of recombinant proteins from both prokaryotes and eukaryotes is reported here, and this secretion signal allows a flexible strategy for the production and secretion in numerous hosts, and to conveniently and rapidly study protein expression.
Some Improved Versions of Methods for the Indirect Detection of Staphylococcal Protein A Gene Expressed in Escherichia coli
- BiologyMicrobiology and immunology
- 1992
After lysis of the transformants grown on a nitrocellulose membrane by alkali, SpA could be directly detected by immuno‐detection procedures after inactivation of endogenous peroxidase in bacteria by phenylhydrazine and hydrogen peroxide.
Production of Soluble Recombinant Proteins in Bacteria
- BiologyNature Biotechnology
- 1989
This review summarizes what is known about why IBs form and ways of increasing the production of soluble protein in bacterial systems and discusses possibilities for mimicking these mechanisms in bacteria via secretion, cloning of mammalian foldases, and mutation of the post-translational modification systems of the host bacteria.
Expression and Fermentation Strategies for Recombinant Protein Production in Escherichia Coli
- Biology
- 2001
The authors consider the influence of the cultivation conditions on the cellular capacity for the production of recombinant proteins in connection to the actual knowledge of the carbon flows, the energy situation, the activity of the protein synthesis apparatus, and the stress responses.
Optimisation of signal peptide for recombinant protein secretion in bacterial hosts
- Biology, EngineeringApplied Microbiology and Biotechnology
- 2013
Several important characteristics and requirements are summarised for the design of a more efficient signal peptide for the production of recombinant proteins in E. coli.
Staphylococcal protein A as a fusion partner directs secretion of the e1alpha and e1beta subunits of pea mitochondrial pyruvate dehydrogenase by Bacillus subtilis.
- BiologyProtein expression and purification
- 2000
The use of SPA as a fusion partner during expression of heterologous proteins by B. subtilis provides the basis of a versatile system that can be used to study both secretion and protein:protein interactions.
The mutability of Staphylococcal biofilms
- Biology
- 2010
The role of oxidative stress in biofilm mutability was investigated by addition of antioxidants to biofilms, and MFs were reduced up to 5-fold, suggesting a role for oxidative damage.
Structural studies of factor B of the alternative pathway of the complement system.
- Medicine
- 2002
Factor B of the complement system is a five-domain, 90 kD serine protease proenzyme which is activated by the protease factor D in the context of the Mg^^-dependent complex C3bB during complement activation and SELDIAMS provides an efficient means of identifying residues involved in protein-protein interactions.
