A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.

The Spumaretrovirinae, or foamyviruses (FVs) are complex retroviruses that infect many species of monkey and ape. Although FV infection is apparently benign, trans-species zoonosis is commonplace and has resulted in the isolation of the Prototypic Foamy Virus (PFV) from human sources and the potenti...

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Autores principales:	David C Goldstone, Thomas G Flower, Neil J Ball, Marta Sanz-Ramos, Melvyn W Yap, Roksana W Ogrodowicz, Nicole Stanke, Juliane Reh, Dirk Lindemann, Jonathan P Stoye, Ian A Taylor
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/bf273cf189fd4945879bcf1e69bf50f8
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spelling	oai:doaj.org-article:bf273cf189fd4945879bcf1e69bf50f82021-11-18T06:05:39ZA unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.1553-73661553-737410.1371/journal.ppat.1003376https://doaj.org/article/bf273cf189fd4945879bcf1e69bf50f82013-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23675305/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The Spumaretrovirinae, or foamyviruses (FVs) are complex retroviruses that infect many species of monkey and ape. Although FV infection is apparently benign, trans-species zoonosis is commonplace and has resulted in the isolation of the Prototypic Foamy Virus (PFV) from human sources and the potential for germ-line transmission. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. In addition, PFV Gag interacts with the FV Envelope (Env) protein to facilitate budding of infectious particles. Presently, there is a paucity of structural information with regards FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. Therefore, in order to probe the functional overlap of FV and orthoretroviral Gag and learn more about FV egress and replication we have undertaken a structural, biophysical and virological study of PFV-Gag. We present the crystal structure of a dimeric amino terminal domain from PFV, Gag-NtD, both free and in complex with the leader peptide of PFV Env. The structure comprises a head domain together with a coiled coil that forms the dimer interface and despite the shared function it is entirely unrelated to either the capsid or matrix of Gag from other retroviruses. Furthermore, we present structural, biochemical and virological data that reveal the molecular details of the essential Gag-Env interaction and in addition we also examine the specificity of Trim5α restriction of PFV. These data provide the first information with regards to FV structural proteins and suggest a model for convergent evolution of gag genes where structurally unrelated molecules have become functionally equivalent.David C GoldstoneThomas G FlowerNeil J BallMarta Sanz-RamosMelvyn W YapRoksana W OgrodowiczNicole StankeJuliane RehDirk LindemannJonathan P StoyeIan A TaylorPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 5, p e1003376 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 David C Goldstone Thomas G Flower Neil J Ball Marta Sanz-Ramos Melvyn W Yap Roksana W Ogrodowicz Nicole Stanke Juliane Reh Dirk Lindemann Jonathan P Stoye Ian A Taylor A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
description	The Spumaretrovirinae, or foamyviruses (FVs) are complex retroviruses that infect many species of monkey and ape. Although FV infection is apparently benign, trans-species zoonosis is commonplace and has resulted in the isolation of the Prototypic Foamy Virus (PFV) from human sources and the potential for germ-line transmission. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. In addition, PFV Gag interacts with the FV Envelope (Env) protein to facilitate budding of infectious particles. Presently, there is a paucity of structural information with regards FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. Therefore, in order to probe the functional overlap of FV and orthoretroviral Gag and learn more about FV egress and replication we have undertaken a structural, biophysical and virological study of PFV-Gag. We present the crystal structure of a dimeric amino terminal domain from PFV, Gag-NtD, both free and in complex with the leader peptide of PFV Env. The structure comprises a head domain together with a coiled coil that forms the dimer interface and despite the shared function it is entirely unrelated to either the capsid or matrix of Gag from other retroviruses. Furthermore, we present structural, biochemical and virological data that reveal the molecular details of the essential Gag-Env interaction and in addition we also examine the specificity of Trim5α restriction of PFV. These data provide the first information with regards to FV structural proteins and suggest a model for convergent evolution of gag genes where structurally unrelated molecules have become functionally equivalent.
format	article
author	David C Goldstone Thomas G Flower Neil J Ball Marta Sanz-Ramos Melvyn W Yap Roksana W Ogrodowicz Nicole Stanke Juliane Reh Dirk Lindemann Jonathan P Stoye Ian A Taylor
author_facet	David C Goldstone Thomas G Flower Neil J Ball Marta Sanz-Ramos Melvyn W Yap Roksana W Ogrodowicz Nicole Stanke Juliane Reh Dirk Lindemann Jonathan P Stoye Ian A Taylor
author_sort	David C Goldstone
title	A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
title_short	A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
title_full	A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
title_fullStr	A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
title_full_unstemmed	A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
title_sort	unique spumavirus gag n-terminal domain with functional properties of orthoretroviral matrix and capsid.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/bf273cf189fd4945879bcf1e69bf50f8
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A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.

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