A. Wierzba et al., PRODUCTION AND PROPERTIES OF A BIFUNCTIONAL FUSION PROTEIN THAT MEDIATES ATTACHMENT OF VERO CELLS TO CELLULOSIC MATRICES, Biotechnology and bioengineering, 47(2), 1995, pp. 147-154
The sequence Arg-Gly-Asp (RGD) in extracellular matrix proteins such a
s fibronectin, collagen, and laminin mediates cell attachment by inter
acting with proteins of the integrin family of cell surface receptors.
A gene fusion encoding the RGD-containing peptide, fused to the C-ter
minus of a cellulose-binding domain (CBD/RGD), was expressed in Escher
ichia coli. Cultures produced up to 50 mg of CBD/RGD per titer, most o
f which was extracellular. it was purified from the culture supernatan
t by affinity chromatography on cellulose. CBD/RGD promoted the attach
ment of green monkey Vero cells to polystyrene and cellulose acetate.
Attachment was inhibited by smalt synthetic peptides containing the RG
D sequence. CBD/RGD was as effective as collagen in promoting the atta
chment of Vero cells to Cellsnow(TM) microcarriers. (C) 1995 John Wile
y and Sons, Inc.