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

Harvard

Pezeshkian, W, Nabo, LJ & Ipsen, JH 2017, 'Cholera toxin B subunit induces local curvature on lipid bilayers', FEBS Open Bio, vol. 7, no. 11, pp. 1638-1645. https://doi.org/10.1002/2211-5463.12321

APA

Pezeshkian, W., Nabo, L. J., & Ipsen, J. H. (2017). Cholera toxin B subunit induces local curvature on lipid bilayers. FEBS Open Bio, 7(11), 1638-1645. https://doi.org/10.1002/2211-5463.12321

Vancouver

Pezeshkian W, Nabo LJ, Ipsen JH. Cholera toxin B subunit induces local curvature on lipid bilayers. FEBS Open Bio. 2017 Nov;7(11):1638-1645. https://doi.org/10.1002/2211-5463.12321

Author

Pezeshkian, Weria ; Nabo, Lina J. ; Ipsen, John H. / Cholera toxin B subunit induces local curvature on lipid bilayers. In: FEBS Open Bio. 2017 ; Vol. 7, No. 11. pp. 1638-1645.

Bibtex

@article{e7b2d934e4ec4324a3b8384022ffce19,
title = "Cholera toxin B subunit induces local curvature on lipid bilayers",
abstract = "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.",
keywords = "endocytosis, ganglioside, peripheral proteins, CLATHRIN-INDEPENDENT ENDOCYTOSIS, MOLECULAR-DYNAMICS METHOD, MEMBRANE INVAGINATIONS, FORCE-FIELD, BINDING, GROMACS, GM1, INTERNALIZATION, IMPLEMENTATION, SIMULATIONS",
author = "Weria Pezeshkian and Nabo, {Lina J.} and Ipsen, {John H.}",
year = "2017",
month = nov,
doi = "10.1002/2211-5463.12321",
language = "English",
volume = "7",
pages = "1638--1645",
journal = "FEBS Open Bio",
issn = "2211-5463",
publisher = "FEBS Press",
number = "11",

}

RIS

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