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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 669-674 |
| Number of pages | 6 |
| Journal | Microbes and Infection |
| Volume | 18 |
| Issue number | 11 |
| DOIs | |
| State | Published - Nov 1 2016 |
Keywords
- CPAF
- Neutralization of antichlamydial activity
- Proteolysis of complement factor C3 & factor B
ASJC Scopus subject areas
- Infectious Diseases
- Microbiology
- Immunology
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