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Recombinant production of genetically modified S-layer proteins in different expression systems
Lederer, F.; Kutschke, S.; Pollmann, K.;
Surface layer (S-layer) are proteins which cover the outermost of many prokaryotes and are probably the basic and oldest forms of bacterial envelope. These proteins are mostly composed of protein and glycoprotein monomers and have the ability to self-assemble into two-dimensional arrays on interfaces. Several characteristics like their work as molecular sieve, as virulence factor or the protection of the cell from toxic heavy metal ions make S-layer proteins interesting for their usage as ultrafiltration membranes, drug microcontainers, filter materials or patterning structures in nanotechnology.
Heterologous expression of S-layer proteins is not simple and depends on the used vector and the expression system. Equally the S-layer protein size, genetic specifics, and the existence of adapted signal peptides influence the expression. To enable an efficient and economical protein production protein secretion is the most favoured method.
In this work we describe the recombinant production of different S-layer variants and characterize the differences of the used protein expression systems.
We used four different S-layer genes of Lysinibacillus sphaericus JG-A12, Bacillus spec. JG-B12 and Lactobacillus acidophilus and expressed their proteins in Escherichia coli, Pichia pastoris and Lactococcus lactis. Some of these proteins were genetically modified to adapt the construct to the used S-layer expression system.
Our work identified Lactococcus lactis as the best expression system for the used S-layer genes.
  • Poster
    Annual Conference of the Association for General and Applied Microbiology (VAAM), 18.-21.03.2012, Tübingen, Deutschland

Publ.-Id: 16513 - Permalink