The effectiveness of toxin-neutralizing antibodies is considered to be mediated through the interaction of the variable region of the antibody and the toxin; however, recent studies suggest that the constant region (Fc) of antibodies also influence efficacy.
In this issue of the Journal of Clinical Investigation , Jeffrey Ravetch and colleagues at The Rockefeller University demonstrate that engineering the Fc domain of anti-toxin antibodies increases toxin neutralization activity through enhancing the interaction between toxin-targeting antibodies and the Fc receptor on immune cells. The authors found that mice expressing humanized FcR were better protected from anthrax toxin when given engineered anti-anthrax toxin antibodies.
This study suggests that engineering the Fc domains of antibodies can be used as a strategy to enhance antibody efficacy.
TITLE: Human IgG Fc domain engineering enhances antitoxin neutralizing antibody activity
AUTHOR CONTACT: Jeffrey V. Ravetch
The Rockefeller University, New York, NY, USA
Phone: 212-327-7323; Fax: ; E-mail: ravetch@rockefeller.edu
View this article at: http://www.jci.org/articles/view/72676?key=2cb7f03d851cec347394
Journal of Clinical Investigation