scholarly journals Fibroblast adhesion to recombinant tropoelastin expressed as a protein A-fusion protein

1991 ◽  
Vol 273 (3) ◽  
pp. 517-522 ◽  
Author(s):  
L E Grosso ◽  
W C Parks ◽  
L J Wu ◽  
R P Mecham
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Fusion Protein ◽  
Developmental Regulation ◽  
Protein A ◽  
Receptor Binding Site ◽  
Elastin Receptor ◽  
Cnbr Cleavage ◽  
Fibroblast Adhesion ◽  
Nuchal Ligament

A bovine tropoelastin cDNA encoding exons 15-36 that includes the elastin-receptor binding site was expressed in Escherichia coli as a fusion protein with Protein A from Staphylococcus aureus. After isolation of the fusion protein by affinity chromatography on Ig-Sepharose, the tropoelastin domain was separated from plasmid-pR1T2T-encoded Protein A (Protein A') by CNBr cleavage. Cell-adhesion assays demonstrated specific adhesion to the recombinant tropoelastin. Furthermore, the data indicate that interactions involving the bovine elastin receptor mediate nuchalligament fibroblast adhesion to the recombinant protein. In agreement with earlier studies of fibroblast chemotaxis to bovine tropoelastin, nuchal-ligament fibroblast adhesion demonstrated developmental regulation of the elastin receptor.

Expression of recombinant human glucose-dependent insulinotropic polypeptide in Escherichia coli by sequence-specific proteolysis of a protein A fusion protein

Peptides ◽  
1990 ◽  
Vol 11 (6) ◽  
pp. 1069-1074 ◽  
Author(s):  
Billy K.-C. Chow ◽  
Glenn W. Morrow ◽  
Margaret Ho ◽  
Raymond A. Pederson ◽  
Christopher H.S. McIntosh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Protein A

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

1998 ◽  
Vol 64 (1) ◽  
pp. 342-345 ◽  
Author(s):  
Lothar Steidler ◽  
Jasmine Viaene ◽  
Walter Fiers ◽  
Erik Remaut
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Fusion Protein ◽  
Lactococcus Lactis ◽  
Heterologous Protein ◽  
Protein A ◽  
Food Grade ◽  
Secretion Signal ◽  
Secretion Signal Peptide ◽  
Polystyrene Support

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 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.

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