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The long half-life of botulinum neurotoxin serotype A (BoNT/A) in cells poses a challenge in developing post-exposure therapeutics complementary to existing antitoxin strategies. Delivery vehicles consisting of the toxin heavy chain (HC), including the receptor-binding domain and translocation domain, connected to an inhibitory cargo offer a possible solution for rescuing intoxicated neurons in victims paralyzed from botulism. Here, we report the expression and purification of soluble recombinant prototype green fluorescent protein (GFP) cargo proteins fused to the entire BoNT/A-HC (residues 544-1295) in Escherichia coli with up to a 40 amino acid linker inserted between the cargo and BoNT/A-HC vehicle. We show that these GFP-HC fusion proteins are functionally active and readily taken up by cultured neuronal cells as well as by neuronal cells in mouse motor nerve endings.

Original publication

DOI

10.1093/protein/gzq093

Type

Journal

Protein engineering, design & selection : PEDS

Publication Date

03/2011

Volume

24

Pages

247 - 253

Addresses

Department of Microbiology, University of Illinois at Urbana-Champaign, Champaign, IL, USA.

Keywords

Toes, Neurons, Motor Neurons, Neuromuscular Junction, Animals, Mice, Escherichia coli, Recombinant Fusion Proteins, Drug Carriers, Reflex, Drug Delivery Systems, Protein Engineering, Protein Structure, Tertiary, Protein Transport, Botulinum Toxins, Type A