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Title: Structural basis for tuning activity and membrane specificity of bacterial cytolysins
Authors: Shah, Nita R
Voisin, Tomas B
Parsons, Edward S
Keywords: Bacterial cytolysins; Cholesterol-dependent cytolysins
Issue Date: 2020
Publisher: Biochemical Journal
Abstract: Cholesterol-dependent cytolysins (CDCs) form protein nanopores to lyse cells. They target eukaryotic cells using different mechanisms, but all require the presence of cholesterol to pierce lipid bilayers. How CDCs use cholesterol to selectively lyse cells is essential for understanding virulence strategies of several pathogenic bacteria, and for repurposing CDCs to kill new cellular targets. Here we address that question by trapping an early state of pore formation for the CDC intermedilysin, bound to the human immune receptor CD59 in a nanodisc model membrane. Our cryo-electron microscopy map reveals structural transitions required for oligomerization, which include the lateral movement of a key amphipathic helix. We demonstrate that the charge of this helix is crucial for tuning lytic activity of CDCs. Furthermore, we discover modifications that overcome the requirement of cholesterol for membrane rupture, which will facilitate engineering the target-cell specificity of pore-forming proteins.
Description: Tài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0
URI: http://dlib.hust.edu.vn/handle/HUST/24079
Link item primary: https://www.biorxiv.org/content/10.1101/2020.06.16.154724v1
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường
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