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

45 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

Access to Document

10.1016/j.bbamem.2010.08.004

Cite this

@article{e3fe86cfb16f40e58b35c8ec9d2d83a8,

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 .",

year = "2011",

month = feb,

doi = "10.1016/j.bbamem.2010.08.004",

language = "English",

volume = "1808",

pages = "572--579",

journal = "Biochimica et Biophysica Acta - Biomembranes",

issn = "0005-2736",

publisher = "Elsevier B.V.",

number = "2",

}

TY - JOUR

T1 - ORF8a of SARS-CoV forms an ion channel

T2 - Experiments and molecular dynamics simulations

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

Y1 - 2011/2

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

UR - https://www.scopus.com/pages/publications/78650287426

U2 - 10.1016/j.bbamem.2010.08.004

DO - 10.1016/j.bbamem.2010.08.004

M3 - Article

C2 - 20708597

AN - SCOPUS:78650287426

SN - 0005-2736

VL - 1808

SP - 572

EP - 579

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

IS - 2

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this