Human monoclonal antibodies that neutralize anthrax toxin by inhibiting heptamer assembly

Article type: Research Article

Authors: Wang, Fei^a | Ruther, Paul^a | Jiang, Ivy^a | Sawada-Hirai, Ritsuko^a | Sun, Shu Man^a | Nedellec, Rebecca^{a; b} | Morrow, Phillip R.^a | Kang, Angray S.^{a; *}

Affiliations: [a] Avanir Pharmaceuticals, Antibody Technology, 11388 Sorrento Valley Rd, San Diego, CA 92121, USA | [b] Current affiliation: Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA

Correspondence: [*] Corresponding author: Avanir Pharmaceuticals, Antibody Technology, 11388 Sorrento Valley Rd, San Diego, California 92121, USA. Tel.: +1 858 622 5294; Fax: +1 858 658 7458; E-mail: [email protected]

Abstract: A panel of human anti-anthrax protective antigen IgG1 monoclonal antibodies were evaluated to determine the mechanism of toxin neutralization. AVP-22G12, AVP-1C6 and AVP-21D9 bound to the protective antigen with picomolar affinities to distinct non-overlapping linear epitopes. Two of the antibodies neutralized the anthrax toxin by completely inhibiting the protective antigen oligomer assembly process in vitro.

Keywords: human monoclonal antibodies, bacillus anthracis, protective antigen

DOI: 10.3233/HAB-2004-13402

Journal: Human Antibodies, vol. 13, no. 4, pp. 105-110, 2004