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Published on: October 25, 2019
Chlamydia pneumoniae inclusion membrane protein Cpn0147 interacts with host protein CREB3
1Laboratory Medicine College, Hebei North University, Zhang Jiakou, Hebei Province, PR China.
Abstract:
Chlamydiae are Gram-negative obligate intracellular bacteria that cause diseases with significant medical and economic impacts. Like other chlamydial species, Chlamydia pneumoniae possesses a unique developmental cycle, the infectious elementary body gains access to the susceptible host cell, where it transforms into the replicative reticulate body. The cytoplasmic vacuole where Chlamydia pneumoniae replicates is called an inclusion, which is extensively modified by the insertion of chlamydial effectors known as inclusion membrane proteins (Incs). The C. pneumoniae-specific inclusion membrane protein (Inc) Cpn0147 contains domains that are predicted to be exposed to the host cytoplasm. To map host cell binding partners of Cpn0147, a yeast two-hybrid system was used to screen Cpn0147 against a HeLa cell cDNA library, which led to the finding that Cpn0147 interacted with the host cell protein cyclic adenosine monophosphate (cAMP)-responsive element (CRE)-binding protein (CREB3). The interaction was validated by co-immunoprecipitation of Cpn0147 with CREB3 from HeLa cells ectopically expressing both. Furthermore, Cpn0147 and CREB3 were co-localised in HeLa cells under confocal fluorescence microscopy. The above observations suggest that CREB3 may directly bind to the cytoplasmic domain of Cpn0147 to mediate the interactions of chlamydial inclusions with host cell endoplasmic reticulum.
Insights
Chlamydia pneumoniae Cpn0147 protein interacts with host CREB3 protein. This interaction may mediate chlamydial inclusions binding to host endoplasmic reticulum, impacting bacterial pathogenesis.
Area of Science:
- Microbiology
- Cell Biology
- Molecular Biology
Background:
- Chlamydiae are Gram-negative obligate intracellular bacteria causing significant diseases.
- Chlamydia pneumoniae has a unique developmental cycle involving elementary and reticulate bodies.
- Chlamydial inclusions are modified by inclusion membrane proteins (Incs) inserted into the vacuole.
Purpose of the Study:
- To identify host cell binding partners of the C. pneumoniae-specific Inc protein, Cpn0147.
- To investigate the interaction between Cpn0147 and host cell proteins.
- To elucidate the role of Cpn0147-host protein interactions in chlamydial pathogenesis.
Main Methods:
- Yeast two-hybrid system screening of Cpn0147 against a HeLa cell cDNA library.
- Co-immunoprecipitation to validate Cpn0147-CREB3 interaction in HeLa cells.
- Confocal fluorescence microscopy to assess co-localization of Cpn0147 and CREB3.
Main Results:
- Cpn0147 was found to interact with the host cell protein CREB3 (cyclic adenosine monophosphate-responsive element-binding protein 3).
- The interaction between Cpn0147 and CREB3 was validated by co-immunoprecipitation.
- Cpn0147 and CREB3 were observed to co-localize within HeLa cells.
Conclusions:
- CREB3 may directly bind to the cytoplasmic domain of Cpn0147.
- This interaction likely mediates the binding of chlamydial inclusions to the host cell endoplasmic reticulum.
- Understanding this interaction provides insights into Chlamydia pneumoniae pathogenesis.
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