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Updated: May 10, 2025

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Pleiotropic functions of CpdB in Bacillus anthracis
Junmin Yao1,2, Shaohuihao Li1,2, Xuefan Wu1,2
1Center for Biosafety Mega-Science, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei, China.
Abstract:
Bacillus anthracis is the causative agent of anthrax disease. Our prior research indicated that cyclic (c)-di-AMP accumulation attenuated bacterial virulence in mice. However, the function of c-di-AMP secretion and its regulatory mechanism in anthrax have not been revealed. We characterized the role of the ecto-nucleotidase CpdB in B. anthracis. CpdB exhibits phosphodiesterase activity towards c-di-AMP and 2'3'-cGMP-AMP, and nucleotidase activity towards several mononucleotides, including the preferred substrates c-di-AMP and pApA. Our results demonstrated that inactivation of cpdB altered purine nucleotide metabolism, decreasing the levels of anthrax toxins and extracellular proteases while increasing the expression of adhesion factor BslA. The rates of adhesion and invasion of B. anthracis to both endothelial cells and immune cells in vitro were enhanced by cpdB inactivation. In infected silkworms, cpdB inactivation led to higher levels of colonization in hemolymph, but virulence was attenuated. These findings suggest that cpdB has pleiotropic functions in the infection and virulence of B. anthracis.
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