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Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of immatu...

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Autores principales: Welker, Lisa, Paillart, Jean-Christophe, Bernacchi, Serena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402826/
https://www.ncbi.nlm.nih.gov/pubmed/34452424
http://dx.doi.org/10.3390/v13081559
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author Welker, Lisa
Paillart, Jean-Christophe
Bernacchi, Serena
author_facet Welker, Lisa
Paillart, Jean-Christophe
Bernacchi, Serena
author_sort Welker, Lisa
collection PubMed
description Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of immature virions at the plasma membrane, were firstly identified within retroviral Gag precursors, and in a further step, also in structural proteins of many other enveloped RNA viruses including arenaviruses, filoviruses, rhabdoviruses, reoviruses, and paramyxoviruses. Three classes of L domains have been identified thus far (PT/SAP, YPXnL/LXXLF, and PPxY), even if it has recently been suggested that other motifs could act as L domains. Here, we summarize the current state of knowledge of the different types of L domains and their cellular partners in the budding events of RNA viruses, with a particular focus on retroviruses.
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spelling pubmed-84028262021-08-29 Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses Welker, Lisa Paillart, Jean-Christophe Bernacchi, Serena Viruses Review Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of immature virions at the plasma membrane, were firstly identified within retroviral Gag precursors, and in a further step, also in structural proteins of many other enveloped RNA viruses including arenaviruses, filoviruses, rhabdoviruses, reoviruses, and paramyxoviruses. Three classes of L domains have been identified thus far (PT/SAP, YPXnL/LXXLF, and PPxY), even if it has recently been suggested that other motifs could act as L domains. Here, we summarize the current state of knowledge of the different types of L domains and their cellular partners in the budding events of RNA viruses, with a particular focus on retroviruses. MDPI 2021-08-06 /pmc/articles/PMC8402826/ /pubmed/34452424 http://dx.doi.org/10.3390/v13081559 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Welker, Lisa
Paillart, Jean-Christophe
Bernacchi, Serena
Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
title Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
title_full Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
title_fullStr Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
title_full_unstemmed Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
title_short Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
title_sort importance of viral late domains in budding and release of enveloped rna viruses
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402826/
https://www.ncbi.nlm.nih.gov/pubmed/34452424
http://dx.doi.org/10.3390/v13081559
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