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J. Bacteriol., 03 1995, 1470-1476, Vol 177, No. 6
Copyright © 1995, American Society for Microbiology

Cell surface display of recombinant proteins on Staphylococcus carnosus

P Samuelson, M Hansson, N Ahlborg, C Andreoni, F Gotz, T Bachi, TN Nguyen, H Binz, M Uhlen and S Stahl
Department of Biochemistry and Biotechnology, Royal Institute of Technology, Stockholm, Sweden.

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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