Matthew Beard

TL;DR: Mutant botulinum neurotoxin B containing E1191M/S1199Y exhibits ~11-fold higher efficacy in blocking neurotransmission than wild-type botulinu toxin B in neurons expressing human synaptotagmin II, demonstrating that enhancing receptor binding increases the overall efficacy at functional levels.

TL;DR: The preclinical characterization of two engineered botulinum neurotoxin serotype B proteins with significant therapeutic potential are reported and it is demonstrated that neuronal surface receptor binding limits the clinical efficacy of unmodified BoNT/B and that modified Bo NT/B proteins have promising clinical potential.

TL;DR: This article discusses site directed mutagenesis, used to affect the biological properties of BoNTs, including approaches to alter their binding to neurons and to alter the specificity and kinetics of substrate cleavage.

TL;DR: Despite lacking the Hc (cell-targeting) domain, LHn/B retained the capacity to internalize and cleave intracellular VAMP-1 and -2 when added to the cells at high concentration.

TL;DR: P purification and characterization of enzymatically active, and of inactive nontoxic, recombinant forms of BoNT/FA are reported as tractable alternatives to purifying this neurotoxin from native Clostridium botulinum.