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Functional display of a heterologous protein on the surface of Lactococcus lactis by means of the cell wall anchor of Staphylococcus aureus protein A

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Abstract
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 Usp-45 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.
Keywords
GRAM-POSITIVE BACTERIA, FIBRONECTIN-BINDING PROTEIN, STREPTOCOCCUS-PYOGENES, NUCLEOTIDE-SEQUENCE, ESCHERICHIA-COLI, CLONING VECTORS, SUBSP LACTIS, GENE, EXPRESSION, LYSOSTAPHIN

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Citation

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Chicago
Steidler, Lothar, Jasmine Viaene, Walter Fiers, and Erik Remaut. 1998. “Functional Display of a Heterologous Protein on the Surface of Lactococcus Lactis by Means of the Cell Wall Anchor of Staphylococcus Aureus Protein A.” Applied and Environmental Microbiology 64 (1): 342–345.
APA
Steidler, L., Viaene, J., Fiers, W., & Remaut, E. (1998). Functional display of a heterologous protein on the surface of Lactococcus lactis by means of the cell wall anchor of Staphylococcus aureus protein A. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 64(1), 342–345.
Vancouver
1.
Steidler L, Viaene J, Fiers W, Remaut E. Functional display of a heterologous protein on the surface of Lactococcus lactis by means of the cell wall anchor of Staphylococcus aureus protein A. APPLIED AND ENVIRONMENTAL MICROBIOLOGY. 1998;64(1):342–5.
MLA
Steidler, Lothar, Jasmine Viaene, Walter Fiers, et al. “Functional Display of a Heterologous Protein on the Surface of Lactococcus Lactis by Means of the Cell Wall Anchor of Staphylococcus Aureus Protein A.” APPLIED AND ENVIRONMENTAL MICROBIOLOGY 64.1 (1998): 342–345. Print.
@article{176037,
  abstract     = {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 Usp-45 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.},
  author       = {Steidler, Lothar and Viaene, Jasmine and Fiers, Walter and Remaut, Erik},
  issn         = {0099-2240},
  journal      = {APPLIED AND ENVIRONMENTAL MICROBIOLOGY},
  keywords     = {GRAM-POSITIVE BACTERIA,FIBRONECTIN-BINDING PROTEIN,STREPTOCOCCUS-PYOGENES,NUCLEOTIDE-SEQUENCE,ESCHERICHIA-COLI,CLONING VECTORS,SUBSP LACTIS,GENE,EXPRESSION,LYSOSTAPHIN},
  language     = {eng},
  number       = {1},
  pages        = {342--345},
  title        = {Functional display of a heterologous protein on the surface of Lactococcus lactis by means of the cell wall anchor of Staphylococcus aureus protein A},
  volume       = {64},
  year         = {1998},
}

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