Abstract

Anthrax, caused by Bacillus anthracis (B anthracis), poses a potential threat as a bioterror agent because after inhalation, the spores rapidly cause bacteraemia and toxaemia. It produces a toxin consisting of three proteins ie protective antigen (PA), oedema factor (EF) and lethal factor (LF). Protective antigen plays a central role in the pathophysiology of anthrax and offers an excellent therapeutic target for treatment of anthrax. Raxibacumab is a recombinant, fully human, IgG1λ monoclonal antibody directed against PA of B anthracis. It inhibits PA binding to the anthrax toxin receptor and inhibits toxin-mediated cell death. It has been approved under animal rule or animal efficacy rule by the United States Food and Drug Administration which comes into play when it is not feasible or ethical to perform controlled clinical trials in humans. It has shown promising results in various animal studies which includes significantly improved survival rates in the raxibacumab group than non-raxibacumab group.

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