Authors: George P. Anderson, Yakelin A. Ortiz-Vera, Andrew Hayhurst, Jill Czarnecki, Jason Dabbs, BaoHan Vo, Ellen R. Goldman
Addresses: Naval Research Laboratory, Center for BioMolecular Science and Engineering, Washington DC, 20375, USA. ' University of Puerto Rico, Biology Department, P.O. Box 4010, Arecibo, PR 00614, USA. ' Southwest Foundation for Biomedical Research, San Antonio, TX 78227-5301, USA. ' Naval Medical Research Center, Biological Defense Research Directorate, Silver Spring, MD 20910, USA. ' Naval Medical Research Center, Biological Defense Research Directorate, Silver Spring, MD 20910, USA. ' Atlanta University, 223 James P. Brawley Drive, SW, Atlanta, GA 30314, USA. ' Naval Research Laboratory, Center for BioMolecular Science and Engineering, Washington, DC 20375, USA
Abstract: Lama immunoglobulins consist of conventional antibody (IgG1) and unique forms that lack light chains, called heavy chain antibodies (IgG2 and IgG3). These unusual antibodies possess unique properties ideal for diagnostics and therapeutics. To evaluate the IgG from a llama immunised with botulinum complex toxoids A through F each IgG subclass was tested as capture and recognition ligand in xMAP fluid array immunoassays. The optimal combination, IgG3 capture and IgG2 tracer, detected as low as 64 pg/ml of BoNT/A complex toxoid. Also, heavy chain antibodies were shown to bind BoNT as effectively as conventional IgG1, while possessing much greater thermal stability. [Received 15 October; Accepted 28 December 2007]
Keywords: llama; heavy chain antibodies; HcAb; immunoglobulins; IgG subclasses; botulinum neurotoxins; Luminex; xMAP fluid array immunoassay; botulism; binding.
The Botulinum Journal, 2008 Vol.1 No.1, pp.100 - 115
Published online: 25 Jun 2008 *Full-text access for editors Full-text access for subscribers Purchase this article Comment on this article