Cholera toxin B subunit induces local curvature on lipid bilayers
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Cholera toxin B subunit induces local curvature on lipid bilayers. / Pezeshkian, Weria; Nabo, Lina J.; Ipsen, John H.
In: FEBS Open Bio, Vol. 7, No. 11, 11.2017, p. 1638-1645.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Cholera toxin B subunit induces local curvature on lipid bilayers
AU - Pezeshkian, Weria
AU - Nabo, Lina J.
AU - Ipsen, John H.
PY - 2017/11
Y1 - 2017/11
N2 - The B subunit of the bacterial cholera toxin (CTxB) is responsible for the toxin binding to the cell membrane and its intracellular trafficking. CTxB binds to the monosialotetrahexosyl ganglioside at the plasma membrane of the target cell and mediates toxin internalization by endocytosis. CTxB induces a local membrane curvature that is essential for its clathrin-independent uptake. Using all-atom molecular dynamics, we show that CTxB induces local curvature, with the radius of curvature around 36 nm. The main feature of the CTxB 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.
AB - The B subunit of the bacterial cholera toxin (CTxB) is responsible for the toxin binding to the cell membrane and its intracellular trafficking. CTxB binds to the monosialotetrahexosyl ganglioside at the plasma membrane of the target cell and mediates toxin internalization by endocytosis. CTxB induces a local membrane curvature that is essential for its clathrin-independent uptake. Using all-atom molecular dynamics, we show that CTxB induces local curvature, with the radius of curvature around 36 nm. The main feature of the CTxB 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.
KW - endocytosis
KW - ganglioside
KW - peripheral proteins
KW - CLATHRIN-INDEPENDENT ENDOCYTOSIS
KW - MOLECULAR-DYNAMICS METHOD
KW - MEMBRANE INVAGINATIONS
KW - FORCE-FIELD
KW - BINDING
KW - GROMACS
KW - GM1
KW - INTERNALIZATION
KW - IMPLEMENTATION
KW - SIMULATIONS
U2 - 10.1002/2211-5463.12321
DO - 10.1002/2211-5463.12321
M3 - Journal article
VL - 7
SP - 1638
EP - 1645
JO - FEBS Open Bio
JF - FEBS Open Bio
SN - 2211-5463
IS - 11
ER -
ID: 316867723