Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli

Bacterial protein secretion is important in the life cycles of most bacteria, in which it contributes to the formation of pili and flagella and makes available extracellular enzymes to digest polymers for nutritional purposes and toxins to kill host cells in infections of humans, animals and plants....

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Bibliographic Details
Published in:Nature biotechnology 2006-01, Vol.24 (1), p.100-104
Main Authors: Weiner, Joel H, Zhang, Guijin, Brokx, Stephen
Format: Article
Language:English
Subjects:
Agriculture
Base Sequence
Bioinformatics
Biological and medical sciences
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
Biomedicine
Biotechnology
Carrier Proteins - genetics
Carrier Proteins - secretion
E coli
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins - genetics
Escherichia coli Proteins - secretion
Extracellular Fluid - metabolism
Fundamental and applied biological sciences. Psychology
Growth conditions
letter
Life cycles
Life Sciences
Molecular Sequence Data
Polymers
Protein Engineering - methods
Proteins
Recombinant Fusion Proteins - secretion
Toxins
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Summary:Bacterial protein secretion is important in the life cycles of most bacteria, in which it contributes to the formation of pili and flagella and makes available extracellular enzymes to digest polymers for nutritional purposes and toxins to kill host cells in infections of humans, animals and plants. It is generally accepted that nonpathogenic laboratory strains of Escherichia coli, particularly K12 strains, do not secrete proteins into the extracellular medium under routine growth conditions. In this study, we report that commonly used laboratory strains secrete YebF, a small (10.8 kDa in the native form), soluble endogenous protein into the medium, challenging the status quo view that laboratory strains do not secrete proteins to the medium. We further show that 'passenger' proteins linked to the carboxyl end of YebF are efficiently secreted. The function of YebF is unknown, but its use as a carrier for transgenic proteins provides a tool to circumvent toxicity and other contamination issues associated with protein production in E. coli.
ISSN:1087-0156
1546-1696
DOI:10.1038/nbt1174