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Published on: July 6, 2016
Identification of histone H2B as a potential receptor for Mycoplasma genitalium protein of adhesion
Yating Liao1, Xiangying Deng1, Kailan Peng1
1Institute of Pathogenic Biology, Hengyang Medical College, University of South China, Hunan Provincial Key Laboratory for Special Pathogens Prevention and Control, Hengyang City, Hunan Province, 421001, P.R. China.
Abstract:
Mycoplasma genitalium, the smallest prokaryotic microorganism capable of independent replication, is increasingly recognized as a sexually transmitted pathogen. M. genitalium protein of adhesion (MgPa) plays a pivotal role in the process of M. genitalium adhesion to host cells. We previously identified cyclophilin A as a cellular receptor of MgPa using the virus overlay protein binding assay (VOPBA) together with liquid chromatography-mass spectrometry (LC-MS). In the current study, we have evaluated H2B as an alternative cellular receptor for MgPa since H2B was assigned the second higher score as a potential binding partner of MgPa in the VOPBA and LC-MS screen. It was found that recombinant MgPa specifically bind to H2B both in the SV-HUC-1 cell membrane and in form of a recombinant protein. H2B was detected throughout the SV-HUC-1 cells, including the cytoplasmic membrane, cytosol and nucleus. Importantly, H2B partially inhibited the adhesion of M. genitalium to SV-HUC-1 cells. Finally, H2B was both co-precipitated with recombinant MgPa and co-localized with M. genitalium and recombinant MgPa in SV-HUC-1 cells. The above observations suggest that H2B may act as a potential cellular receptor of MgPa for mediating M. genitalium adhesion to host cells.
Insights
Histone H2B is identified as a potential cellular receptor for Mycoplasma genitalium adhesion. This finding suggests H2B may play a role in how this sexually transmitted pathogen attaches to host cells.
Area of Science:
- Microbiology
- Cell Biology
- Infectious Diseases
Background:
- Mycoplasma genitalium is a growing concern as a sexually transmitted pathogen.
- The M. genitalium protein of adhesion (MgPa) is crucial for host cell attachment.
- Previous research identified cyclophilin A as an MgPa receptor.
Purpose of the Study:
- To investigate Histone H2B (H2B) as a potential alternative cellular receptor for MgPa.
- To elucidate the role of H2B in M. genitalium adhesion to host cells.
Main Methods:
- Virus overlay protein binding assay (VOPBA) and liquid chromatography-mass spectrometry (LC-MS) screening.
- Binding assays using recombinant MgPa and H2B in SV-HUC-1 cells.
- Immunofluorescence microscopy for H2B localization and co-localization studies.
- Co-precipitation assays to confirm protein interactions.
- Functional assays to assess H2B's effect on M. genitalium adhesion.
Main Results:
- Recombinant MgPa specifically binds to H2B in cell membranes and as a recombinant protein.
- H2B is localized within SV-HUC-1 cells, including cytoplasmic membrane, cytosol, and nucleus.
- H2B partially inhibited M. genitalium adhesion to SV-HUC-1 cells.
- H2B co-precipitated with recombinant MgPa and co-localized with M. genitalium in host cells.
Conclusions:
- Histone H2B is a potential cellular receptor for MgPa.
- H2B may mediate the adhesion of Mycoplasma genitalium to host cells, offering a new target for therapeutic strategies.
