Structural model of the SARS coronavirus E channel in LMPG micelles

Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which...

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Main Authors: Surya, Wahyu, Li, Yan, Torres, Jaume
Other Authors: School of Biological Sciences
Format: Journal Article
Language:English
Published: 2019
Subjects:
Online Access:https://hdl.handle.net/10356/105338
http://hdl.handle.net/10220/48644
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author Surya, Wahyu
Li, Yan
Torres, Jaume
author2 School of Biological Sciences
author_facet School of Biological Sciences
Surya, Wahyu
Li, Yan
Torres, Jaume
author_sort Surya, Wahyu
collection NTU
description Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.
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spelling ntu-10356/1053382023-02-28T17:02:13Z Structural model of the SARS coronavirus E channel in LMPG micelles Surya, Wahyu Li, Yan Torres, Jaume School of Biological Sciences DRNTU::Science::Biological sciences Envelope Protein Solution NMR Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation. MOE (Min. of Education, S’pore) Accepted version 2019-06-11T09:15:41Z 2019-12-06T21:49:24Z 2019-06-11T09:15:41Z 2019-12-06T21:49:24Z 2018 Journal Article Surya, W., Li, Y., & Torres, J. (2018). Structural model of the SARS coronavirus E channel in LMPG micelles. Biochimica et Biophysica Acta - Biomembranes, 1860(6), 1309-1317. doi:10.1016/j.bbamem.2018.02.017 0005-2736 https://hdl.handle.net/10356/105338 http://hdl.handle.net/10220/48644 10.1016/j.bbamem.2018.02.017 en Biochimica et Biophysica Acta - Biomembranes © 2018 Elsevier B.V. All rights reserved. This paper was published in Biochimica et Biophysica Acta - Biomembranes and is made available with permission of Elsevier B.V. 22 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences
Envelope Protein
Solution NMR
Surya, Wahyu
Li, Yan
Torres, Jaume
Structural model of the SARS coronavirus E channel in LMPG micelles
title Structural model of the SARS coronavirus E channel in LMPG micelles
title_full Structural model of the SARS coronavirus E channel in LMPG micelles
title_fullStr Structural model of the SARS coronavirus E channel in LMPG micelles
title_full_unstemmed Structural model of the SARS coronavirus E channel in LMPG micelles
title_short Structural model of the SARS coronavirus E channel in LMPG micelles
title_sort structural model of the sars coronavirus e channel in lmpg micelles
topic DRNTU::Science::Biological sciences
Envelope Protein
Solution NMR
url https://hdl.handle.net/10356/105338
http://hdl.handle.net/10220/48644
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