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Mycoplasma genitalium Protein of Adhesion Promotes the Early Proliferation of Human Urothelial Cells by Interacting
Pei Dai1, Xiangying Deng1, Peng Liu1
1Hunan Provincial Key Laboratory for Special Pathogens Prevention and Control, Hunan Province Cooperative Innovation Center for Molecular Target New Drug Study, Institute of Pathogenic Biology, Hengyang Medical College, University of South China, Hengyang 421001, China.
Abstract:
Mycoplasma genitalium is a newly recognized pathogen associated with sexually transmitted diseases (STDs). MgPa, the adhesion protein of Mycoplasma genitalium, is the main adhesin and the key factor for M. genitalium interacting with host cells. Currently, the long-term survival mechanism of M. genitalium in the host is not clear. In this study, a T7 phage-displayed human urothelial cell (SV-HUC-1) cDNA library was constructed, and the interaction of MgPa was screened from this library using the recombinant MgPa (rMgPa) as a target molecule. We verified that 60S ribosomal protein L35 (RPL35) can interact with MgPa using far-Western blot and co-localization analysis. According to the results of tandem mass tag (TMT) labeling and proteome quantitative analysis, there were altogether 407 differentially expressed proteins between the pcDNA3.1(+)/MgPa-transfected cells and non-transfected cells, of which there were 6 downregulated proteins and 401 upregulated proteins. The results of qRT-PCR demonstrated that interaction between rMgPa and RPL35 could promote the expressions of EIF2, SRP68, SERBP1, RPL35A, EGF, and TGF-β. 3-(4,5)-Dimethylthiahiazo(-z-y1)-3,5-di-phenytetrazoliumromide bromide (MTT) assays corroborated that the interaction between rMgPa and RPL35 could promote SV-HUC-1 cell proliferation. Therefore, our findings indicated that the interaction between rMgPa and RPL35 can enhance the expressions of transcription-initiation and translation-related proteins and thus promote cell proliferation. This study elucidates a new biological function of MgPa and can explain this new mechanism of M. genitalium in the host.
Insights
Mycoplasma genitalium adhesion protein MgPa interacts with human ribosomal protein RPL35, promoting cell proliferation and offering insights into pathogen survival mechanisms.
Area of Science:
- Microbiology and Immunology
- Cell Biology
- Molecular Biology
Background:
- Mycoplasma genitalium is a sexually transmitted pathogen.
- The adhesion protein MgPa is crucial for host cell interaction.
- The survival mechanisms of M. genitalium in hosts remain unclear.
Purpose of the Study:
- To identify host factors interacting with MgPa.
- To elucidate the role of MgPa-host interactions in M. genitalium survival.
- To understand the functional consequences of MgPa binding to host proteins.
Main Methods:
- Construction of a T7 phage-displayed human urothelial cell cDNA library.
- Screening for MgPa interacting proteins using recombinant MgPa (rMgPa).
- Verification via far-Western blot and co-localization analysis.
- Proteomic analysis using tandem mass tag (TMT) labeling.
- Gene expression analysis using qRT-PCR.
- Cell proliferation assays (MTT).
Main Results:
- Identified 60S ribosomal protein L35 (RPL35) as an interacting partner of MgPa.
- Proteomic analysis revealed 401 upregulated and 6 downregulated proteins in MgPa-transfected cells.
- Interaction between rMgPa and RPL35 upregulated transcription and translation-related genes (EIF2, SRP68, SERBP1, RPL35A, EGF, TGF-β).
- MgPa-RPL35 interaction promoted SV-HUC-1 cell proliferation.
Conclusions:
- The interaction between MgPa and RPL35 enhances the expression of transcription and translation factors.
- This interaction promotes host cell proliferation, potentially aiding M. genitalium survival.
- A novel biological function of MgPa is elucidated, explaining a potential host colonization mechanism.
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