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

Jordi Naval, Jaume Piñol, Xavier Rebordosa, Xavier Serra-Hartmann, Josep A. Pérez-Pons, Enrique Querol

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Abstract

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.
Original languageEnglish
Pages (from-to)288-294
JournalProtein Expression and Purification
Volume9
DOIs
Publication statusPublished - 1 Jan 1997

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