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Appl Environ Microbiol, January 1998, p. 342-345, Vol. 64, No. 1
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Functional Display of a Heterologous Protein on the Surface of Lactococcus lactis by Means of the Cell Wall Anchor of Staphylococcus aureus Protein A

Lothar Steidler, Jasmine Viaene, Walter Fiers, and Erik Remaut*

Flanders Interuniversity Institute for Biotechnology, Department of Molecular Biology, Universiteit Gent, B-9000 Ghent, Belgium

Received 22 July 1997/Accepted 17 October 1997

In this study, we showed that the cell wall anchor of protein A from Staphylococcus aureus is functional in the food-grade organism Lactococcus lactis. A fusion protein composed of the lactococcal Usp45 secretion signal peptide, streptavidin monomer, and the S. aureus protein A anchor became covalently attached to the peptidoglycan when expressed in L. lactis. The streptavidin moiety of the fusion protein was functionally exposed at the cellular surface. L. lactis cells expressing the anchored fusion polypeptide could be specifically immobilized on a biotinylated alkaline phosphatase-coated polystyrene support.

* Corresponding author. Mailing address: Laboratory of Molecular Biology, Universiteit Gent, K. L. Ledeganckstraat 35, B-9000 Ghent, Belgium. Phone: 32 9 264 5130. Fax: 32 9 264 5330. E-mail: erik.remaut{at}lmb1.rug.ac.be.




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