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Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
Published on: August 25, 2013
Sphingomyelin trafficking in Chlamydia pneumoniae-infected cells
1Host-Parasite Interactions Section, Laboratory of Intracellular Parasites, National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, Hamilton, MT 59840, USA.
Abstract:
Chlamydia pneumoniae is a bacterial obligate intracellular parasite with a developmental cycle common to all members of the genus Chlamydia. Like other chlamydiae, the developmental cycle of C. pneumoniae occurs entirely within a membrane-bound intracellular vacuole, termed an inclusion, that is non-fusogenic with endosomal or lysosomal compartments. To characterize the vesicular interactions of the C. pneumoniae inclusion, we used a fluorescent analogue of ceramide, (N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproyl-Derythro-sphingosine (C6-NBD-Cer), that has previously been used to characterize the endogenous synthesis and transport of sphingolipids from the Golgi apparatus to Chlamydia trachomatis and Chlamydia psittaci inclusions. Sphingolipids are trafficked to C. pneumoniae inclusions in a time-, temperature- and energy-dependent manner with properties very similar to the delivery of sphingomyelin to C. trachomatis inclusions. These results indicate that interactions of the inclusion with a subset of sphingomyelin-containing exocytic vesicles is a property common to all species of chlamydiae.
Insights
Chlamydia pneumoniae inclusions interact with specific vesicles containing sphingolipids. This interaction is essential for the bacteria
Area of Science:
- Microbiology
- Cell Biology
Background:
- Chlamydia pneumoniae is an obligate intracellular parasite.
- Its developmental cycle occurs within a non-fusogenic vacuole (inclusion).
Purpose of the Study:
- To characterize the vesicular interactions of the C. pneumoniae inclusion.
- To investigate sphingolipid transport to the inclusion.
Main Methods:
- Used a fluorescent ceramide analogue (C6-NBD-Cer).
- Analyzed sphingolipid transport to C. pneumoniae inclusions.
Main Results:
- Sphingolipids are trafficked to C. pneumoniae inclusions.
- Transport is time-, temperature-, and energy-dependent.
- Inclusion interactions resemble those of C. trachomatis.
Conclusions:
- C. pneumoniae inclusions interact with sphingomyelin-containing exocytic vesicles.
- This interaction is a common property among Chlamydia species.
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