PE_PGRS3 ensures provision of the vital phospholipids cardiolipin and phosphatidylinositols by promoting the interaction between M. tuberculosis and host cells
| العنوان: | PE_PGRS3 ensures provision of the vital phospholipids cardiolipin and phosphatidylinositols by promoting the interaction between M. tuberculosis and host cells |
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| المؤلفون: | Giovanni Delogu, Eliza Kramarska, Rita Berisio, Massimiliano Papi, Flavio De Maio, Ivana Palucci, Valentina Palmieri, Michela Sali, Silvia Bellesi, Alessandro Salustri, Federica Marchionni, Maurizio Sanguinetti, Basem Battah |
| المصدر: | Virulence, Vol 12, Iss 1, Pp 868-884 (2021) Virulence |
| بيانات النشر: | Informa UK Limited, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Microbiology (medical), phosphatidylinositols, Immunology, Infectious and parasitic diseases, RC109-216, Biology, pe_pgrs, Microbiology, Settore MED/07 - MICROBIOLOGIA E MICROBIOLOGIA CLINICA, Pathogenesis, Mycobacterium tuberculosis, 03 medical and health sciences, chemistry.chemical_compound, Cardiolipin, Phosphatidylinositol, PE_PGRS, adhesion, host interaction, tuberculosis, 030304 developmental biology, 0303 health sciences, 030306 microbiology, Mycobacterium smegmatis, Phosphate, biology.organism_classification, Cell biology, Infectious Diseases, chemistry, Phosphorylation, Parasitology, Heterologous expression |
| الوصف: | PE_PGRS proteins ofMycobacterium tuberculosis(Mtb) constitute a large family of complex modular proteins whose role is still unclear. Among those, we have previously shown, using the heterologous expression inMycobacterium smegmatis, that PE_PGRS3 containing a unique arginine-rich C-terminal domain, promotes adhesion to host cells. In this study, we investigate the role of PE_PGRS3 and its C-terminal domain directly inMtbusing functional deletion mutants. The results obtained here show that PE_PGRS3 is localized on the mycobacterial cell wall and its arginine-rich C-terminal region protrudes from the mycobacterial membrane and mediatesMtbentry into epithelial cells. Most importantly, this positively charged helical domain specifically binds phosphorylated phosphatidylinositols and cardiolipin, whereas it is unable to bind other phospholipids. Interestingly, administration of cardiolipin and phosphatidylinositol but no other phospholipids was able to turn-off expression ofpe_pgrs3 activated by phosphate starvation conditions. These findings suggest that PE_PGRS3 has the key role to serve as a bridge between mycobacteria and host cells by interacting with specific host phospholipids and extracting them from host cells, for their direct integration or as a source of phosphate, during phases of TB pathogenesis whenMtbis short of phosphate supply. |
| تدمد: | 2150-5608 2150-5594 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd34c59be82ec8db0981c7d8513ebc99Test https://doi.org/10.1080/21505594.2021.1897247Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....fd34c59be82ec8db0981c7d8513ebc99 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 21505608 21505594 |
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