ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations

Cheng Chang Chen; Jens Krüger; Issara Sramala; Hao Jen Hsu; Peter Henklein; Yi Ming Arthur Chen; Wolfgang B. Fischer

doi:10.1016/j.bbamem.2010.08.004

ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations

Cheng Chang Chen, Jens Krüger, Issara Sramala, Hao Jen Hsu, Peter Henklein, Yi Ming Arthur Chen, Wolfgang B. Fischer

Institute of Biophotonics

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

Abstract

ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9 ± 0.8 pS at elevated temperature (38.5 °C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.

Original language	English
Pages (from-to)	572-579
Number of pages	8
Journal	Biochimica et Biophysica Acta - Biomembranes
Volume	1808
Issue number	2
DOIs	https://doi.org/10.1016/j.bbamem.2010.08.004
State	Published - Feb 2011

Keywords

Bilayer recording
Ion channel
Molecular dynamics
ORF8a
SARS-CoV

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10.1016/j.bbamem.2010.08.004

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title = "ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations",

abstract = "ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9 ± 0.8 pS at elevated temperature (38.5 °C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.",

keywords = "Bilayer recording, Ion channel, Molecular dynamics, ORF8a, SARS-CoV",

author = "Chen, {Cheng Chang} and Jens Kr{\"u}ger and Issara Sramala and Hsu, {Hao Jen} and Peter Henklein and Chen, {Yi Ming Arthur} and Fischer, {Wolfgang B.}",

note = "Funding Information: WBF acknowledges the National Yang-Ming University and the Government of Taiwan for financial support (Aim of Excellence Program), as well as the National Science Council of Taiwan (NSC) . JK acknowledges a fellowship granted jointly by the Alexander von Humboldt-Foundation and NSC .",

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AU - Chen, Cheng Chang

AU - Krüger, Jens

AU - Sramala, Issara

AU - Hsu, Hao Jen

AU - Henklein, Peter

AU - Chen, Yi Ming Arthur

AU - Fischer, Wolfgang B.

N1 - Funding Information: WBF acknowledges the National Yang-Ming University and the Government of Taiwan for financial support (Aim of Excellence Program), as well as the National Science Council of Taiwan (NSC) . JK acknowledges a fellowship granted jointly by the Alexander von Humboldt-Foundation and NSC .

PY - 2011/2

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N2 - ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9 ± 0.8 pS at elevated temperature (38.5 °C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.

AB - ORF8a protein is 39 residues long and contains a single transmembrane domain. The protein is synthesized using solid phase peptide synthesis and reconstituted into artificial lipid bilayers that forms cation-selective ion channels with a main conductance level of 8.9 ± 0.8 pS at elevated temperature (38.5 °C). Computational modeling studies including multi nanosecond molecular dynamics simulations in a hydrated POPC lipid bilayer are done with a 22 amino acid transmembrane helix to predict a putative homooligomeric helical bundle model. A structural model of a pentameric bundle is proposed with cysteines, serines and threonines facing the pore.

KW - Bilayer recording

KW - Ion channel

KW - Molecular dynamics

KW - ORF8a

KW - SARS-CoV

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JF - Biochimica et Biophysica Acta - Biomembranes

IS - 2

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ORF8a of SARS-CoV forms an ion channel: Experiments and molecular dynamics simulations

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Keywords

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