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 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.
Naval
J
J
Institut de Biologia Fonamental, Universitat Autònoma de Barcelona, Bellaterra, Spain.
Piñol
J
J
Rebordosa
X
X
Serra-Hartmann
X
X
Pérez-Pons
J A
JA
Querol
E
E
D015153:Blotting, Western; D003001:Cloning, Molecular; D004274:DNA, Recombinant; D004926:Escherichia coli / Q000235:genetics*; D015707:HN Protein; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D018112:Respiratory Syncytial Virus, Bovine / Q000737:chemistry / Q000235:genetics*; D012995:Solubility; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification*; D014764:Viral Proteins / Q000096:biosynthesis* / Q000302:isolation & purification*
D004274:DNA, Recombinant; D015707:HN Protein; D011993:Recombinant Fusion Proteins; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; C116204:attachment protein G