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Article type: Research Article
Authors: Wang, Feia | Ruther, Paula | Jiang, Ivya | Sawada-Hirai, Ritsukoa | Sun, Shu Mana | Nedellec, Rebeccaa; 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: fwang@avanir.com
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
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