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Potent neutralization of anthrax edema toxin by a humanized monoclonal antibody that competes with calmodulin for edema factor binding.

Authors

Chen Z, Moayeri M, Zhao H, Crown D, Leppla SH, Purcell RH.

Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. zchen@niaid.nih.gov

Abstract

This study describes the isolation and characterization of a neutralizing monoclonal antibody (mAb) against anthrax edema factor, EF13D. EF13D neutralized edema toxin (ET)-mediated cyclic AMP (cAMP) responses in cells and protected mice from both ET-induced footpad edema and systemic ET-mediated lethality. The antibody epitope was mapped to domain IV of EF. The mAb was able to compete with calmodulin (CaM) for EF binding and displaced CaM from EF-CaM complexes. EF-mAb binding affinity (0.05-0.12 nM) was 50- to 130-fold higher than that reported for EF-CaM. This anti-EF neutralizing mAb could potentially be used alone or with an anti-PA mAb in the emergency prophylaxis and treatment of anthrax infection.

References

  • Chen Z, Moayeri M, Zhao H, Crown D, Leppla SH, Purcell RH. Potent neutralization of anthrax edema toxin by a humanized monoclonal antibody that competes with calmodulin for edema factor binding. Proc. Natl. Acad. Sci. U.S.A. 2009;106;32
  • PubMed id : 19651602
  • doi : 10.1073/pnas.0906581106

Link to pubmed | Link to Google Scholar | Link to full text publication

2009


Proceedings of the National Academy of Sciences of the United States of America


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