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. 1995 Mar;177(6):1470–1476. doi: 10.1128/jb.177.6.1470-1476.1995

Cell surface display of recombinant proteins on Staphylococcus carnosus.

P Samuelson 1, M Hansson 1, N Ahlborg 1, C Andréoni 1, F Götz 1, T Bächi 1, T N Nguyen 1, H Binz 1, M Uhlén 1, S Ståhl 1
PMCID: PMC176761  PMID: 7883702

Abstract

A novel expression system for surface display of heterologous proteins on Staphylococcus carnosus cells has been developed. Taking advantage of the promoter and secretion signals, including a propeptide region, from the lipase gene of Staphylococcus hyicus and the cell wall-spanning and membrane-binding region of protein A from Staphylococcus aureus, efficient surface display of an 80-amino-acid peptide from a malaria blood stage antigen could be achieved. A serum albumin binding protein from streptococcal protein G was used both as a general reporter molecule and to increase the accessibility of the surface-displayed proteins. Immunoblotting, immunogold staining, and immunofluorescence on intact recombinant S. carnosus cells verified the presence of the propeptide, the malaria antigen, and the albumin-binding reporter protein on the bacterial surface. For the first time, fluorescence-activated cell sorting was used to analyze the presence of surface-displayed hybrid receptors on gram-positive bacteria.

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Selected References

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