CtHtrA: the lynchpin of the chlamydial surface and a promising therapeutic target

Future Microbiol. 2017 Jul:12:817-829. doi: 10.2217/fmb-2017-0017. Epub 2017 Jun 8.

Abstract

Chlamydia trachomatis is the most prevalent sexually transmitted bacterial infection worldwide and the leading cause of preventable blindness. Reports have emerged of treatment failure, suggesting a need to develop new antibiotics to battle Chlamydia infection. One possible candidate for a new treatment is the protease inhibitor JO146, which is an effective anti-Chlamydia agent that targets the CtHtrA protein. CtHtrA is a lynchpin on the chlamydial cell surface due to its essential and multifunctional roles in the bacteria's stress response, replicative phase of development, virulence and outer-membrane protein assembly. This review summarizes the current understanding of CtHtrA function and presents a mechanistic model that highlights CtHtrA as an effective target for anti-Chlamydia drug development.

Keywords: DegP; HtrA; intracellular; protease; virulence.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Anti-Bacterial Agents / therapeutic use
  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / metabolism
  • Chlamydia Infections / drug therapy*
  • Chlamydia Infections / microbiology
  • Chlamydia trachomatis / drug effects
  • Chlamydia trachomatis / enzymology*
  • Chlamydia trachomatis / metabolism
  • Chlamydia trachomatis / pathogenicity
  • Dipeptides / therapeutic use
  • Humans
  • Models, Biological
  • Models, Molecular
  • Organophosphonates / therapeutic use
  • Protease Inhibitors / pharmacology
  • Protease Inhibitors / therapeutic use
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*
  • Virulence Factors / chemistry
  • Virulence Factors / metabolism

Substances

  • Anti-Bacterial Agents
  • Bacterial Outer Membrane Proteins
  • Dipeptides
  • JO146 compound
  • Organophosphonates
  • Protease Inhibitors
  • Virulence Factors
  • Serine Endopeptidases