The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness

-. Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. -. Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Nt(out)-Ct(in) membr...

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Autores principales: Duart, Gerard, García-Murria, Maria J., Mingarro, Ismael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Authors. Published by Elsevier B.V. 2021
Materias:
BBA Research Letter
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7987508/
https://www.ncbi.nlm.nih.gov/pubmed/33771486
http://dx.doi.org/10.1016/j.bbamem.2021.183608
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author Duart, Gerard
García-Murria, Maria J.
Mingarro, Ismael
author_facet Duart, Gerard
García-Murria, Maria J.
Mingarro, Ismael
author_sort Duart, Gerard
collection PubMed
description -. Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. -. Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Nt(out)-Ct(in) membrane topology. -. E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2.
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spelling pubmed-79875082021-03-24 The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness Duart, Gerard García-Murria, Maria J. Mingarro, Ismael Biochim Biophys Acta Biomembr BBA Research Letter -. Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. -. Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Nt(out)-Ct(in) membrane topology. -. E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2. The Authors. Published by Elsevier B.V. 2021-07-01 2021-03-24 /pmc/articles/PMC7987508/ /pubmed/33771486 http://dx.doi.org/10.1016/j.bbamem.2021.183608 Text en © 2021 The Authors Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle BBA Research Letter
Duart, Gerard
García-Murria, Maria J.
Mingarro, Ismael
The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
title The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
title_full The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
title_fullStr The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
title_full_unstemmed The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
title_short The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
title_sort sars-cov-2 envelope (e) protein has evolved towards membrane topology robustness
topic BBA Research Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7987508/
https://www.ncbi.nlm.nih.gov/pubmed/33771486
http://dx.doi.org/10.1016/j.bbamem.2021.183608
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