Expression inEscherichia coliand 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-c2Escherichia coliexpression vector and expressed as C-terminal maltose-binding protein (MBP) fusion products. The resulting polypeptides were partially soluble and single-step purified by affini...

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Bibliographic Details
Published in:Protein expression and purification 1997-03, Vol.9 (2), p.288-294
Main Authors: Naval, Jordi, Piñol, Jaume, Rebordosa, Xavier, Serra-Hartmann, Xavier, Pérez-Pons, Josep A., Querol, Enrique
Format: Article
Language:English
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Summary:Six fragments of the F gene from bovine respiratory syncytial virus (BRSV) were engineered into the pMAL-c2Escherichia coliexpression 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
1096-0279
DOI:10.1006/prep.1996.0688