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Transmembrane transport and human health
Transport of molecules across biological membranes is vital for all life forms. My research focuses on the specialized trans-membranal proteins that facilitate this process. I aim to understand how these molecular machines are built and how they function. I am especially interested in systems that are relevant to human health, such as bacterial transport systems that play central roles in host-pathogen interactions. In some of the deadliest pathogens, these systems are crucial for bacterial colonization and progression of disease. Over the years, my lab has shed light on their operation and proposed novel inhibitory strategies.
Another focus is diseases resulting from faulty transmembrane transport. Cystic fibrosis, a common hereditary disease, arises from mutations in the CFTR protein, a chloride channel. Collaborating with Professor Haliloglu from Boğaziçi University, Turkey, we developed a computational method identifying druggable sites for allosteric modulation. Applying this to CFTR revealed a new druggable allosteric hotspot, which may be used to restore CFTR activity and mitigate cystic fibrosis symptoms.
Selected Publications
ˆ Ersoy A, Altintel B, Livnat Levanon N, Ben-Tal N, Haliloglu T*, Lewinson O*. (2023). Computational analysis of long-range allosteric communications in CFTR. Elife. 2023 18;12:RP88659. doi: 10.7554/eLife.88659. * Corresponding authors
ˆ Yang M*, Livnat Levanon N*, Acar B, Aykac Fas B, Masrati G, Rose J, Ben-Tal
N, Haliloglu T, Zhao Y, Lewinson O. Single-molecule probing of the conformational homogeneity of the ABC transporter BtuCD. Nature Chemical Biology. 2018 14(7):715- 722. doi: 10.1038/s41589-018-0088-2. *equal contribution
lewinson@technion.ac.il
Oded Lewinson Lab
Oded Lewinson, PhD
Associate Professor of Molecular Microbiology
PhD, 2005 – Weizmann Institute of Science, Israel
30-31
MOLECULAR MICROBIOLOGY
Identification of a novel druggable allosteric site in the human cystic fibrosis protein