Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases

Virulence. 2021 Dec;12(1):766-787. doi: 10.1080/21505594.2021.1889812.

Abstract

Bacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can respond to new environments presenting stressful conditions. For S. pneumoniae, the human nasopharynx is its natural habitat. In the context of virulence, movement of S. pneumoniae to the lungs, blood, or other sites can instigate responses by the bacteria that result in their proteases serving dual roles of self-protein processors and virulence factors of host protein targets.

Keywords: Peptidase; Streptococcus pneumoniae; protease; proteinase; virulence.

Publication types

  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / immunology
  • Bacterial Proteins / metabolism
  • Genome, Bacterial
  • Humans
  • Immune Evasion
  • Lung / microbiology
  • Mice
  • Nasopharynx / microbiology
  • Peptide Hydrolases / genetics
  • Peptide Hydrolases / metabolism*
  • Streptococcus pneumoniae / enzymology*
  • Streptococcus pneumoniae / immunology*
  • Streptococcus pneumoniae / pathogenicity*
  • Virulence
  • Virulence Factors

Substances

  • Bacterial Proteins
  • Virulence Factors
  • Peptide Hydrolases