Bacillus anthracis secretes a three component exotoxin-complex, which contributes to anthrax pathogenesis. Formation of this complex starts with the binding of protective antigen (PA) to its cellular receptor. In this study, we report that PA is a calcium-dependent serine protease and that the protein potentially uses this proteolytic activity for receptor binding. Additionally our findings shed new light on previous research describing the inhibition of anthrax toxins and exotoxin formation. Importantly, inhibition of the proteolytic activity of protective antigen could be a novel therapeutic strategy in fighting B. anthracis-related infections.

Additional Metadata
Keywords ANTXR1/2 receptor, B. anthracis, Calcium, Protective antigen, Serine protease
Persistent URL dx.doi.org/10.1080/21505594.2018.1486139, hdl.handle.net/1765/111716
Journal Virulence
Citation
Storm, L. (Lisanne), Bikker, F.J, Nazmi, K, Hulst, A.G, Der Riet-Van Oeveren, D.V. (Debora V.), Veerman, E.C.I, … Kaman, W.E. (2018). Anthrax protective antigen is a calcium-dependent serine protease. Virulence, 9(1), 1085–1091. doi:10.1080/21505594.2018.1486139