Expression inEscherichia coliand Purification of Soluble Forms of the F Protein of Bovine Respiratory Syncytial Virus

Autor: Naval, Jordi, Piñol, Jaume, Rebordosa, Xavier, Serra-Hartmann, Xavier, Pérez-Pons, Josep A., Querol, Enrique
Zdroj: Protein Expression and Purification; March 1997, Vol. 9 Issue: 2 p288-294, 7p
Abstrakt: 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.
Databáze: Supplemental Index