Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.

The matrix protein VP40 coordinates numerous functions in the viral life cycle of the Ebola virus. These range from the regulation of viral transcription to morphogenesis, packaging and budding of mature virions. Similar to the matrix proteins of other nonsegmented, negative-strand RNA viruses, VP40...

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Autores principales:	Leslie P Silva, Michael Vanzile, Sina Bavari, J M Javad Aman, David C Schriemer
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/892a8c2207f84b72b95beb16fa2802c3
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spelling	oai:doaj.org-article:892a8c2207f84b72b95beb16fa2802c32021-11-18T07:13:24ZAssembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.1932-620310.1371/journal.pone.0039978https://doaj.org/article/892a8c2207f84b72b95beb16fa2802c32012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22792204/?tool=EBIhttps://doaj.org/toc/1932-6203The matrix protein VP40 coordinates numerous functions in the viral life cycle of the Ebola virus. These range from the regulation of viral transcription to morphogenesis, packaging and budding of mature virions. Similar to the matrix proteins of other nonsegmented, negative-strand RNA viruses, VP40 proceeds through intermediate states of assembly (e.g. octamers) but it remains unclear how these intermediates are coordinated with the various stages of the life cycle. In this study, we investigate the molecular basis of synchronization as governed by VP40. Hydrogen/deuterium exchange mass spectrometry was used to follow induced structural and conformational changes in VP40. Together with computational modeling, we demonstrate that both extreme N and C terminal tail regions stabilize the monomeric state through a direct association. The tails appear to function as a latch, released upon a specific molecular trigger such as RNA ligation. We propose that triggered release of the tails permits the coordination of late-stage events in the viral life cycle, at the inner membrane of the host cell. Specifically, N-tail release exposes the L-domain motifs PTAP/PPEY to the transport and budding complexes, whereas triggered C-tail release could improve association with the site of budding.Leslie P SilvaMichael VanzileSina BavariJ M Javad AmanDavid C SchriemerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e39978 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Leslie P Silva Michael Vanzile Sina Bavari J M Javad Aman David C Schriemer Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.
description	The matrix protein VP40 coordinates numerous functions in the viral life cycle of the Ebola virus. These range from the regulation of viral transcription to morphogenesis, packaging and budding of mature virions. Similar to the matrix proteins of other nonsegmented, negative-strand RNA viruses, VP40 proceeds through intermediate states of assembly (e.g. octamers) but it remains unclear how these intermediates are coordinated with the various stages of the life cycle. In this study, we investigate the molecular basis of synchronization as governed by VP40. Hydrogen/deuterium exchange mass spectrometry was used to follow induced structural and conformational changes in VP40. Together with computational modeling, we demonstrate that both extreme N and C terminal tail regions stabilize the monomeric state through a direct association. The tails appear to function as a latch, released upon a specific molecular trigger such as RNA ligation. We propose that triggered release of the tails permits the coordination of late-stage events in the viral life cycle, at the inner membrane of the host cell. Specifically, N-tail release exposes the L-domain motifs PTAP/PPEY to the transport and budding complexes, whereas triggered C-tail release could improve association with the site of budding.
format	article
author	Leslie P Silva Michael Vanzile Sina Bavari J M Javad Aman David C Schriemer
author_facet	Leslie P Silva Michael Vanzile Sina Bavari J M Javad Aman David C Schriemer
author_sort	Leslie P Silva
title	Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.
title_short	Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.
title_full	Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.
title_fullStr	Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.
title_full_unstemmed	Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.
title_sort	assembly of ebola virus matrix protein vp40 is regulated by latch-like properties of n and c terminal tails.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/892a8c2207f84b72b95beb16fa2802c3
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Assembly of Ebola virus matrix protein VP40 is regulated by latch-like properties of N and C terminal tails.

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