Secretion of human epidermal growth factor by Corynebacterium glutamicum

  title={Secretion of human epidermal growth factor by Corynebacterium glutamicum},
  author={M Date and Hiroshi Itaya and Hiroshi Matsui and Yoshimi Kikuchi},
  journal={Letters in Applied Microbiology},
  • M. Date, H. Itaya, Y. Kikuchi
  • Published 1 January 2006
  • Biology, Medicine, Engineering, Chemistry
  • Letters in Applied Microbiology
Aims:  To examine the secretion of human epidermal growth factor (hEGF) by Corynebacterium glutamicum. 
Expression of a fusion protein containing human epidermal growth factor and the collagen-binding domain of Vibrio mimicus metalloprotease
The results suggest that recombinant hEGF protein fused to VMCBD may be able to remain for a long period at injured epidermal tissue acting as a healing agent.
Secretion of Streptomyces mobaraensis pro-transglutaminase by coryneform bacteria
These findings suggest that some other coryneform bacteria, especially C. ammoniagenes ATCC6872, are potential hosts for industrial scale protein production, and most c Coryneform species secreted pro-transglutaminase efficiently.
Effects of EGTA on cell surface structures of Corynebacterium glutamicum
It is suggested that EGTA treatment causes release and proteolysis of the CspB protein, resulting in increased cell surface permeability, which is the first report suggesting the importance of calcium ions in cell surface integrity of C. glutamicum.
Desarrollo de herramientas para la producción de proteínas recombinantes en Corynebacterium glutamicum
Fil: Ravasi, Pablo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquimicas y Farmaceuticas. Instituto de Procesos Biotecnologicos y Quimicos de Rosario (IPROBYQ-CONICET); Argentina.
Protein secretion in Corynebacterium glutamicum
In the present review, recent progress in the secretory production of heterologous proteins is critically discussed and the mechanisms of the protein translocation process in C. glutamicum are examined.
Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum
The successful secretion of PG via the recently discovered twin-arginine translocation (Tat) pathway confirms that the Tat pathway of C. glutamicum is an efficient alternative for the industrial-scale production of proteins that are not efficiently secreted by other systems.
Recombinant Protein Expression System in Corynebacterium glutamicum and Its Application
The recent studies on the heterologous expression of the recombinant protein in C. glutamicum are summarized and the advances in genetic components such as promoters, surface anchoring systems, and secretory signal sequences in the bacterium are outlined for effective recombinantprotein expression.
High-level secretory production of recombinant single-chain variable fragment (scFv) in Corynebacterium glutamicum
A new secretory production system for the enhanced production of a single-chain variable fragment (scFv) against the anthrax toxin in Corynebacterium glutamicum is described, and the first report of a fed-batch cultivation for antibody fragment production in C. glutamum is reported.
Proteomics of corynebacteria: From biotechnology workhorses to pathogens
This review focuses on the technical advances made in proteomics approaches during the last years and summarizes applications of these techniques with respect to C. glutamicum metabolic pathways and stress response.
Development of a new platform for secretory production of recombinant proteins in Corynebacterium glutamicum
This is the first report of the development of an efficient secretory expression system by secretome analysis under high cell density cultivation conditions in C. glutamicum, and a new signal peptide is isolated that mediates the efficient secretion of recombinant proteins under highcelldensity cultivation conditions.


Use of Bacillus brevis for efficient synthesis and secretion of human epidermal growth factor.
Using previously isolated Bacillus brevis strains that secrete large amounts of proteins but little protease into the medium, we have developed a host-vector system for very efficient synthesis and
Production of Native-Type Streptoverticillium mobaraense Transglutaminase in Corynebacterium glutamicum
This work has used site-directed mutagenesis to generate an optimal SAM-P45 cleavage site in the C-terminal region of the prodomain of Corynebacterium glutamicum, and native-type transglutaminase was secreted.
Bacillus brevis, a host bacterium for efficient extracellular production of useful proteins.
Although it took many years to explore the new technology, this work succeeded in constructing an excellent host-vector system for producing foreign proteins, using protein-hyperproducing Bacillus brevis as the host.
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major
Industrial production of amino acids by coryneform bacteria.
  • T. Hermann
  • Biology, Engineering
    Journal of biotechnology
  • 2003
Secretion of Active-Form Streptoverticillium mobaraense Transglutaminase by Corynebacterium glutamicum: Processing of the Pro-Transglutaminase by a Cosecreted Subtilisin-Like Protease from Streptomyces albogriseolus
Findings suggest that C. glutamicum has potential as a host for industrial-scale protein production and the transglutaminase gene, secreted by Streptoverticillium mobaraense, is a useful enzyme in the food industry.
Secretory and extracellular production of recombinant proteins using Escherichia coli
  • J. Choi, S. Y. Lee
  • Biology, Engineering
    Applied Microbiology and Biotechnology
  • 2004
Recent advances in secretory and extracellular production of recombinant proteins using E. coli are discussed, including the twin-arginine translocation system, which has recently been employed for the efficient secretion of folded proteins.
Protein secretion in Bacillus species.
Comparison of the presently known export components of Bacillus species with those of Escherichia coli suggests that the mechanism of protein translocation across the cytoplasmic membrane is conserved among gram-negative and gram-positive bacteria differences are found in steps preceding and following the translocation process.