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New structural insights into the multifunctional influenza A matrix protein 1

Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full‐length M1 and...

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Detalles Bibliográficos
Autores principales: Peukes, Julia, Xiong, Xiaoli, Briggs, John A. G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8835727/
https://www.ncbi.nlm.nih.gov/pubmed/34547821
http://dx.doi.org/10.1002/1873-3468.14194
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author Peukes, Julia
Xiong, Xiaoli
Briggs, John A. G.
author_facet Peukes, Julia
Xiong, Xiaoli
Briggs, John A. G.
author_sort Peukes, Julia
collection PubMed
description Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full‐length M1 and show that it assembles filaments in vitro via an interface between the N‐ and C‐terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.
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spelling pubmed-88357272022-02-14 New structural insights into the multifunctional influenza A matrix protein 1 Peukes, Julia Xiong, Xiaoli Briggs, John A. G. FEBS Lett Review Article Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full‐length M1 and show that it assembles filaments in vitro via an interface between the N‐ and C‐terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell. John Wiley and Sons Inc. 2021-10-02 2021-10 /pmc/articles/PMC8835727/ /pubmed/34547821 http://dx.doi.org/10.1002/1873-3468.14194 Text en © 2021 MRC Laboratory of Molecular Biology. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Peukes, Julia
Xiong, Xiaoli
Briggs, John A. G.
New structural insights into the multifunctional influenza A matrix protein 1
title New structural insights into the multifunctional influenza A matrix protein 1
title_full New structural insights into the multifunctional influenza A matrix protein 1
title_fullStr New structural insights into the multifunctional influenza A matrix protein 1
title_full_unstemmed New structural insights into the multifunctional influenza A matrix protein 1
title_short New structural insights into the multifunctional influenza A matrix protein 1
title_sort new structural insights into the multifunctional influenza a matrix protein 1
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8835727/
https://www.ncbi.nlm.nih.gov/pubmed/34547821
http://dx.doi.org/10.1002/1873-3468.14194
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