1887

Abstract

is a versatile pathogen of humans and a continued public health concern due to the rise and spread of multidrug-resistant strains. As part of an ongoing investigation into the pathogenic mechanisms of this organism we previously demonstrated that an intracellular N-terminal processing protease is required for virulence. Following on from this, here we examine the role of CtpA, the lone C-terminal processing protease of . CtpA, a member of the S41 family, is a serine protease whose homologues in Gram-negative bacteria have been implicated in a range of biological functions, including pathogenesis. We demonstrate that CtpA is localized to the bacterial cell wall and expression of the gene is maximal upon exposure to conditions encountered during infection. Disruption of the gene leads to decreased heat tolerance and increased sensitivity when exposed to components of the host immune system. Finally we demonstrate that the mutant strain is attenuated for virulence in a murine model of infection. Our results represent the first characterization of a C-terminal processing protease in a pathogenic Gram-positive bacterium and show that it plays a critical role during infection.

Funding
This study was supported by the:
  • National Institute of Allergies and Infectious Diseases (Award AI109389 and AI080626)
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/content/journal/micro/10.1099/mic.0.079798-0
2014-08-01
2021-07-30
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