Key result
A chimeric beta-galactosidase displaying the foot-and-mouth disease virus cell adhesion peptide successfully bound to and was internalized by mammalian cell lines, remaining transiently active.
Short adhesion peptides of viral origin can function as cell attachment tags to direct the targeted delivery and internalization of functional enzymes into mammalian cells.
Extends viral peptide tags to functional enzyme delivery in mammalian cells; leaves open in vivo therapeutic translation.
The G-H loop of foot-and-mouth disease virus is a disordered protrusion of the VP1 protein exposed on the virion surface. This short stretch includes an arginine-glycine-aspartic acid tripeptide, a recognized integrin-binding motif, which is responsible for cell attachment and infection. Eight copies of a peptide reproducing the amino acid sequence of this FMDV ligand have been displayed in solvent-exposed regions on an enzymatically active recombinant beta-galactosidase. This viral peptide segment enables the chimeric enzyme to bind mammalian cell lines with different efficiencies, probably depending on the number of suitable cell receptors present on each of them. Moreover, it also promotes the internalization of the attached enzyme, which is transiently active inside the cells. These results suggest further exploration of the potential use of short adhesion peptides of viral origin as cell attachment tags to direct the targeted delivery of both genes and enzymes, instead of whole, infectious viruses.
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Villaverde et al. (1998) studied this question. Chimeric enzyme with foot-and-mouth disease virus cell adhesion peptide was evaluated on Binding and internalization into mammalian cell lines. A chimeric beta-galactosidase displaying the foot-and-mouth disease virus cell adhesion peptide successfully bound to and was internalized by mammalian cell lines, remaining transiently active.
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