Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress

ABSTRACT The human cytomegalovirus virion is composed of a DNA genome packaged in an icosahedral capsid, surrounded by a tegument of protein and RNA, all enclosed within a glycoprotein-studded envelope. Achieving this intricate virion architecture requires a coordinated process of assembly and egres...

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Autores principales:	Andrew Womack, Thomas Shenk
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2010
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/c41ec5e696d94a21b038f72e1145fa2e
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spelling	oai:doaj.org-article:c41ec5e696d94a21b038f72e1145fa2e2021-11-15T15:38:17ZHuman Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress10.1128/mBio.00282-102150-7511https://doaj.org/article/c41ec5e696d94a21b038f72e1145fa2e2010-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00282-10https://doaj.org/toc/2150-7511ABSTRACT The human cytomegalovirus virion is composed of a DNA genome packaged in an icosahedral capsid, surrounded by a tegument of protein and RNA, all enclosed within a glycoprotein-studded envelope. Achieving this intricate virion architecture requires a coordinated process of assembly and egress. We show here that pUL71, a component of the virion tegument with a previously uncharacterized function, is required for the virus-induced reorganization of host cell membranes, which is necessary for efficient viral assembly and egress. A mutant that did not express pUL71 was able to efficiently accumulate viral genomes and proteins that were tested but was defective for the production and release of infectious virions. The protein localized to vesicular structures at the periphery of the viral assembly compartment, and during infection with a pUL71-deficient virus, these structures were grossly enlarged and aberrantly contained a cellular marker of late endosomes/lysosomes. Mutant virus preparations exhibited less infectivity per unit genome than wild-type virus preparations, due to aggregation of virus particles and their association with membrane fragments. Finally, mutant virus particles accumulated within the cytoplasm of infected cells and were localized to the periphery of large structures with properties of lysosomes, whose formation was kinetically favored in mutant-virus-infected cells. Together, these observations point to a role for pUL71 in the establishment and/or maintenance of a functional viral assembly compartment that is required for normal virion trafficking and egress from infected cells. IMPORTANCE In addition to causing disease in immunocompromised individuals, human cytomegalovirus is the leading known infectious cause of birth defects. To induce these pathologies, the virus must spread from its site of introduction to various organs and tissues in the body. The processes of viral assembly and egress, which underlie the spread of infection, are incompletely understood. We elucidate a role for a virus-coded protein, pUL71, in these processes and demonstrate the importance of maintaining an intricate, virus-induced reorganization of host cell membranes for efficient virus spread.Andrew WomackThomas ShenkAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 1, Iss 5 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Andrew Womack Thomas Shenk Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress
description	ABSTRACT The human cytomegalovirus virion is composed of a DNA genome packaged in an icosahedral capsid, surrounded by a tegument of protein and RNA, all enclosed within a glycoprotein-studded envelope. Achieving this intricate virion architecture requires a coordinated process of assembly and egress. We show here that pUL71, a component of the virion tegument with a previously uncharacterized function, is required for the virus-induced reorganization of host cell membranes, which is necessary for efficient viral assembly and egress. A mutant that did not express pUL71 was able to efficiently accumulate viral genomes and proteins that were tested but was defective for the production and release of infectious virions. The protein localized to vesicular structures at the periphery of the viral assembly compartment, and during infection with a pUL71-deficient virus, these structures were grossly enlarged and aberrantly contained a cellular marker of late endosomes/lysosomes. Mutant virus preparations exhibited less infectivity per unit genome than wild-type virus preparations, due to aggregation of virus particles and their association with membrane fragments. Finally, mutant virus particles accumulated within the cytoplasm of infected cells and were localized to the periphery of large structures with properties of lysosomes, whose formation was kinetically favored in mutant-virus-infected cells. Together, these observations point to a role for pUL71 in the establishment and/or maintenance of a functional viral assembly compartment that is required for normal virion trafficking and egress from infected cells. IMPORTANCE In addition to causing disease in immunocompromised individuals, human cytomegalovirus is the leading known infectious cause of birth defects. To induce these pathologies, the virus must spread from its site of introduction to various organs and tissues in the body. The processes of viral assembly and egress, which underlie the spread of infection, are incompletely understood. We elucidate a role for a virus-coded protein, pUL71, in these processes and demonstrate the importance of maintaining an intricate, virus-induced reorganization of host cell membranes for efficient virus spread.
format	article
author	Andrew Womack Thomas Shenk
author_facet	Andrew Womack Thomas Shenk
author_sort	Andrew Womack
title	Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress
title_short	Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress
title_full	Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress
title_fullStr	Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress
title_full_unstemmed	Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress
title_sort	human cytomegalovirus tegument protein pul71 is required for efficient virion egress
publisher	American Society for Microbiology
publishDate	2010
url	https://doaj.org/article/c41ec5e696d94a21b038f72e1145fa2e
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Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion Egress

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