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Real-time visualization of perforin nanopore assembly
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Journal Article
Real-time visualization of perforin nanopore assembly
2017
Overview
Perforin is a key protein of the vertebrate immune system. Secreted by cytotoxic lymphocytes as soluble monomers, perforin can self-assemble into oligomeric pores of 10–20 nm inner diameter in the membranes of virus-infected and cancerous cells. These large pores facilitate the entry of pro-apoptotic granzymes, thereby rapidly killing the target cell. To elucidate the pathways of perforin pore assembly, we carried out real-time atomic force microscopy and electron microscopy studies. Our experiments reveal that the pore assembly proceeds via a membrane-bound prepore intermediate state, typically consisting of up to approximately eight loosely but irreversibly assembled monomeric subunits. These short oligomers convert to more closely packed membrane nanopore assemblies, which can subsequently recruit additional prepore oligomers to grow the pore size.
Perforin monomers self-assemble into pre-pores that first insert into the membrane and then recruit additional subunits to grow in size.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Animals
/ Assembly
/ Erythrocyte Membrane - chemistry
/ Erythrocyte Membrane - metabolism
/ Erythrocyte Membrane - ultrastructure
/ Lipids
/ Mice
/ Monomers
/ Nanotechnology and Microengineering
/ Pore Forming Cytotoxic Proteins - chemistry
/ Pore Forming Cytotoxic Proteins - genetics
/ Pore Forming Cytotoxic Proteins - metabolism
/ Pores
/ Porosity
/ Proteins
/ Sheep
