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Updated: Jun 19, 2026
10:32
Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis
Published on: June 10, 2020
Rab6 and Rab11 regulate Chlamydia trachomatis development and golgin-84-dependent Golgi fragmentation
Anette Rejman Lipinski1, Julia Heymann, Charlotte Meissner
1Department of Molecular Biology, Max Planck Institute for Infection Biology, Berlin, Germany.
Plos Pathogens
|October 10, 2009
Summary
Chlamydia infections rely on Rab6 and Rab11 proteins to maintain Golgi stability and nutrient transport. Disrupting these Rab proteins impairs pathogen development and infectious particle formation.
Area of Science:
- Cell Biology
- Microbiology
- Molecular Biology
Background:
- Intracellular pathogens manipulate host cell trafficking pathways, often targeting small GTPases like Rab proteins.
- Chlamydiaceae are known to recruit specific Rab proteins to their inclusions, but their functional significance remains unclear.
Purpose of the Study:
- To investigate the role of Rab proteins in Chlamydia infections.
- To determine the involvement of Rab6 and Rab11 in Chlamydia-induced Golgi fragmentation and nutrient transport.
Main Methods:
- RNA interference (RNAi) was used to deplete specific Rab proteins (Rab6, Rab11) and Golgi matrix components (golgin-84, p115).
- Chlamydia propagation, infectious particle formation, Golgi structure, and nutrient transport (using BODIPY-Ceramide) were assessed in depleted cells.
Main Results:
- Depletion of Rab6 or Rab11 significantly reduced infectious particle formation and inhibited nutrient transport to Chlamydia inclusions.
- Silencing Rab6 or Rab11 prevented Chlamydia-induced Golgi fragmentation and golgin-84 knockdown-stimulated Golgi disruption.
- p115-induced Golgi fragmentation could partially rescue Chlamydia propagation in Rab6 and Rab11 knockdown cells.
Conclusions:
- Rab6 and Rab11 are crucial regulators of Golgi stability during Chlamydia infection.
- Chlamydia subverts the host cell's Golgi structure via Rab proteins to facilitate its intracellular development and nutrient acquisition.
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