Neutralizing antichlamydial activity of complement by chlamydia-secreted protease CPAF

Microbes Infect. 2016 Nov;18(11):669-674. doi: 10.1016/j.micinf.2016.07.002. Epub 2016 Jul 18.

Abstract

Ascending infection by sexually transmitted Chlamydia trachomatis is required for chlamydial induction of tubal pathology. To achieve ascension, the C. trachomatis organisms may have to spread from cell to cell, which inevitably exposes the organisms to extracellular mucosal effectors such as complement factors that are known to possess strong antichlamydial activities. Here, we report that the chlamydia-secreted protease CPAF efficiently neutralized complement factor C3-dependent antichlamydial activity. The neutralization was dependent on the proteolytic activity of CPAF and correlated with the CPAF-mediated degradation of complement factor C3 and factor B. As a result, CPAF preferentially inhibited the alternative complement activation pathway. The significance and limitation of these observations were discussed.

Keywords: CPAF; Neutralization of antichlamydial activity; Proteolysis of complement factor C3 & factor B.

MeSH terms

  • Chlamydia trachomatis / immunology*
  • Complement C3 / antagonists & inhibitors*
  • Complement Factor B / antagonists & inhibitors*
  • Complement Pathway, Alternative
  • Endopeptidases / immunology*
  • HeLa Cells
  • Humans
  • Immune Evasion*
  • Immunologic Factors / antagonists & inhibitors*
  • Proteolysis

Substances

  • Complement C3
  • Immunologic Factors
  • Endopeptidases
  • Complement Factor B
  • CPA factor