Evaluation of anti-hemagglutinin Hn-33 single domain antibodies: kinetics, binding epitopes, and thermal stability
by George P. Anderson, Dan Zabetakis, Rachael D. Bernstein, Shuowei Cai, Bal Ram Singh, Ellen R. Goldman
The Botulinum J. (TBJ), Vol. 2, No. 1, 2011

Abstract: Botulinum Neurotoxin A (BoNT/A) is produced by Clostridium botulinum as a complex with Neurotoxin-Associated Proteins (NAPs) which protect the toxin from proteases and promote adsorption in the gut. Hemagglutinin 33 (Hn-33) makes up the largest fraction of NAPs in the BoNT/A complex. We characterised single domain antibodies (sdAb) which bind Hn-33; the dissociation constant (Kd) varied from 3.8 × 10⁻⁹ M to 1.3 × 10⁻¹⁰ M. Sandwich assays showed that the six sdAb bind two distinct epitopes on Hn-33. Circular dichroism was used to monitor sdAb's secondary structure, thermal denaturing upon heating and rapid refolding upon cooling.

Online publication date: Sat, 06-Aug-2011

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