J. Naval et al., EXPRESSION IN ESCHERICHIA-COLI AND PURIFICATION OF SOLUBLE FORMS OF THE F-PROTEIN OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, Protein expression and purification, 9(2), 1997, pp. 288-294
Six fragments of the F gene from bovine respiratory syncytial virus (B
RSV) were engineered into the pMAL-c2 Escherichia coli expression vect
or and expressed as C-terminal maltose-binding protein (MBP) fusion pr
oducts. The resulting polypeptides were partially soluble and single-s
tep purified by affinity chromatography. These fusion proteins were re
cognized in Western blots by several MAbs directed against human respi
ratory syncytial virus F protein. In addition, rabbit polyclonal antis
era raised against two purified MBP-derived proteins reacted with the
BRSV-F protein. (C) 1997 Academic Press.