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

Lothar Steidler | Zendy; Jasmine Viaene | Zendy; Walter Fiers | Zendy; Erik Remaut | Zendy

Open Access

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

Author(s) -

Lothar Steidler,

Jasmine Viaene,

Walter Fiers,

Erik Remaut

Publication year - 1998

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.64.1.342-345.1998

Subject(s) - lactococcus lactis , biotinylation , peptidoglycan , staphylococcus aureus , streptavidin , nisin , fusion protein , biochemistry , microbiology and biotechnology , biology , chemistry , cell wall , biotin , bacteria , antimicrobial , recombinant dna , lactic acid , genetics , gene

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research