Secretion of human epidermal growth factor by Corynebacterium glutamicum

@article{Date2006SecretionOH,
  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},
  year={2006},
  volume={42}
}
  • 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
TLDR
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
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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
TLDR
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
TLDR
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
TLDR
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
TLDR
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
TLDR
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
TLDR
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
TLDR
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.
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