Genmab elucidates HuMax-EGFr mechanism

Copenhagen, Denmark-based biotechnology firm Genmab AS has made new discoveries into the novel mechanisms of action of its antibody HuMax-EGFr (zalutumumab). By using protein tomography, a new technology that employs an electron microscope to view the three-dimensional structure of proteins on the surface of cells, HuMax-EGFr was shown to lock the epidermal growth factor receptor in an inactive conformation which prevents activation and the binding of growth factors.

Furthermore, the firm stated that HuMax-EGFr inhibits EGF receptor signaling by preventing receptor dimerization and notes that all of these mechanisms have the potential to interfere with cancer cell growth.

"Coupled with previous findings that HuMax-EGFr is able to induce potent antibody-dependent cell-mediated cytotoxicity and block growth factor binding to EGF receptors, these studies have given us greater insight into the novel way HuMax-EGFr works," said Lisa Drakeman, Genmab's chief executive. The data were presented at the 3rd Novel Solution Seminar for Drug Creation and Development in Tokyo, Japan on March 12.