Expression in Escherichia coli and purification of soluble forms of the F protein of bovine respiratory syncytial virus

Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2 Escherichia coli expression vector and expressed as C-terminal maltose-binding protein (MBP) fusion products. The resulting polypeptides were partially soluble and single-step purified by affi...

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Bibliographic Details
Published in:Protein expression and purification 1997-03, Vol.9 (2), p.288-294
Main Authors: Naval, J, Piñol, J, Rebordosa, X, Serra-Hartmann, X, Pérez-Pons, J A, Querol, E
Format: Article
Language:English
Subjects:
Blotting, Western
Cloning, Molecular
DNA, Recombinant
Escherichia coli - genetics
HN Protein
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - isolation & purification
Respiratory Syncytial Virus, Bovine - chemistry
Respiratory Syncytial Virus, Bovine - genetics
Solubility
Viral Envelope Proteins
Viral Fusion Proteins - biosynthesis
Viral Fusion Proteins - genetics
Viral Fusion Proteins - isolation & purification
Viral Proteins - biosynthesis
Viral Proteins - isolation & purification
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Summary:Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2 Escherichia coli expression vector and expressed as C-terminal maltose-binding protein (MBP) fusion products. The resulting polypeptides were partially soluble and single-step purified by affinity chromatography. These fusion proteins were recognized in Western blots by several MAbs directed against human respiratory syncytial virus F protein. In addition, rabbit polyclonal antisera raised against two purified MBP-derived proteins reacted with the BRSV-F protein.
ISSN:1046-5928
DOI:10.1006/prep.1996.0688