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- W3130337336 abstract "In bacteria, the outer membrane constitutes a protective barrier against noxious compounds present in the environment and represents the bacteria's first line of defense against stressors in the environment, including antibiotics. Thereby, understanding the mechanisms by which this barrier is synthesized and regulated is crucial for the fight against antibiotic resistance. In Gram-negative bacteria, lipids are one of the main components of the inner and outer membranes, and their transport requires multiple lipid transporters. The Mla system from E. coli is a transporter which belongs to the MCE (Mammalian Cell Entry) protein family and is implicated in the transport of lipids between the inner and outer membrane of the bacterium. The Mla system is a multi-component system composed of an inner membrane ABC transporter complex, MlaFEDB, an outer membrane complex, MlaA-OmpC/F, and a periplasmic protein, MlaC, which shuttles lipids between the two complexes. Despite the fact that the structures of all components are known, many questions remain unknown. Among them, the direction of lipid transport and the role of ATP in the transport mechanism have been the subject of debate. Also, the mechanism by which lipids are inserted to/extracted from the membranes and how MlaC binds to the inner and outer membrane complexes have not been elucidated. By combining in vitro/in vivo functional assays and biophysical techniques which allow to measure protein-protein interactions, I am working to understand how phospholipids are transported from one membrane complex to another and how interactions occur between the different partners. This study will provide insights into lipid transfer and the mechanisms of outer membrane maintenance." @default.
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- W3130337336 date "2021-02-01" @default.
- W3130337336 modified "2023-10-18" @default.
- W3130337336 title "Understanding the Mechanism of Lipid Transport through the Mla System in E. coli" @default.
- W3130337336 doi "https://doi.org/10.1016/j.bpj.2020.11.1426" @default.
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