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In this study, we showed that the cell wall anchor of protein A fromStaphylococcus aureus is functional in the food-grade organismLactococcus lactis . A fusion protein composed of the lactococcal Usp45 secretion signal peptide, streptavidin monomer, and theS. aureus protein A anchor became covalently attached to the peptidoglycan when expressed inL. 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.

applied and environmental microbiology

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

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