Open AccessCholera toxin B subunit induces local curvature on lipid bilayers
Author(s) -
Pezeshkian Weria,
Nåbo Lina J.,
Ipsen John H.
Publication year - 2017
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12321
Subject(s) - cholera toxin , internalization , ganglioside , endocytosis , membrane curvature , biophysics , lipid bilayer , microbiology and biotechnology , protein subunit , membrane , chemistry , cell membrane , intracellular , toxin , lipid raft , biology , cell , biochemistry , gene
The B subunit of the bacterial cholera toxin (CTxB) is responsible for the toxin binding to the cell membrane and its intracellular trafficking. CT xB binds to the monosialotetrahexosyl ganglioside at the plasma membrane of the target cell and mediates toxin internalization by endocytosis. CT xB induces a local membrane curvature that is essential for its clathrin‐independent uptake. Using all‐atom molecular dynamics, we show that CT xB induces local curvature, with the radius of curvature around 36 nm. The main feature of the CT xB molecular structure that causes membrane bending is the protruding alpha helices in the middle of the protein. Our study points to a generic protein design principle for generating local membrane curvature through specific binding to their lipid anchors.