Virion assembly factories in the nucleus of polyomavirus-infected cells.

Most DNA viruses replicate in the cell nucleus, although the specific sites of virion assembly are as yet poorly defined. Electron microscopy on freeze-substituted, plastic-embedded sections of murine polyomavirus (PyV)-infected 3T3 mouse fibroblasts or mouse embryonic fibroblasts (MEFs) revealed tu...

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Autores principales:	Kimberly D Erickson, Cedric Bouchet-Marquis, Katie Heiser, Eva Szomolanyi-Tsuda, Rabinarayan Mishra, Benjamin Lamothe, Andreas Hoenger, Robert L Garcea
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/93985274bfbb4d58a415fc676e06b4ba
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spelling	oai:doaj.org-article:93985274bfbb4d58a415fc676e06b4ba2021-11-18T06:04:33ZVirion assembly factories in the nucleus of polyomavirus-infected cells.1553-73661553-737410.1371/journal.ppat.1002630https://doaj.org/article/93985274bfbb4d58a415fc676e06b4ba2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22496654/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Most DNA viruses replicate in the cell nucleus, although the specific sites of virion assembly are as yet poorly defined. Electron microscopy on freeze-substituted, plastic-embedded sections of murine polyomavirus (PyV)-infected 3T3 mouse fibroblasts or mouse embryonic fibroblasts (MEFs) revealed tubular structures in the nucleus adjacent to clusters of assembled virions, with virions apparently "shed" or "budding" from their ends. Promyelocytic leukemia nuclear bodies (PML-NBs) have been suggested as possible sites for viral replication of polyomaviruses (BKV and SV40), herpes simplex virus (HSV), and adenovirus (Ad). Immunohistochemistry and FISH demonstrated co-localization of the viral T-antigen (Tag), PyV DNA, and the host DNA repair protein MRE11, adjacent to the PML-NBs. In PML⁻/⁻ MEFs the co-localization of MRE11, Tag, and PyV DNA remained unchanged, suggesting that the PML protein itself was not responsible for their association. Furthermore, PyV-infected PML⁻/⁻ MEFs and PML⁻/⁻ mice replicated wild-type levels of infectious virus. Therefore, although the PML protein may identify sites of PyV replication, neither the observed "virus factories" nor virus assembly were dependent on PML. The ultrastructure of the tubes suggests a new model for the encapsidation of small DNA viruses.Kimberly D EricksonCedric Bouchet-MarquisKatie HeiserEva Szomolanyi-TsudaRabinarayan MishraBenjamin LamotheAndreas HoengerRobert L GarceaPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 4, p e1002630 (2012)
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 Kimberly D Erickson Cedric Bouchet-Marquis Katie Heiser Eva Szomolanyi-Tsuda Rabinarayan Mishra Benjamin Lamothe Andreas Hoenger Robert L Garcea Virion assembly factories in the nucleus of polyomavirus-infected cells.
description	Most DNA viruses replicate in the cell nucleus, although the specific sites of virion assembly are as yet poorly defined. Electron microscopy on freeze-substituted, plastic-embedded sections of murine polyomavirus (PyV)-infected 3T3 mouse fibroblasts or mouse embryonic fibroblasts (MEFs) revealed tubular structures in the nucleus adjacent to clusters of assembled virions, with virions apparently "shed" or "budding" from their ends. Promyelocytic leukemia nuclear bodies (PML-NBs) have been suggested as possible sites for viral replication of polyomaviruses (BKV and SV40), herpes simplex virus (HSV), and adenovirus (Ad). Immunohistochemistry and FISH demonstrated co-localization of the viral T-antigen (Tag), PyV DNA, and the host DNA repair protein MRE11, adjacent to the PML-NBs. In PML⁻/⁻ MEFs the co-localization of MRE11, Tag, and PyV DNA remained unchanged, suggesting that the PML protein itself was not responsible for their association. Furthermore, PyV-infected PML⁻/⁻ MEFs and PML⁻/⁻ mice replicated wild-type levels of infectious virus. Therefore, although the PML protein may identify sites of PyV replication, neither the observed "virus factories" nor virus assembly were dependent on PML. The ultrastructure of the tubes suggests a new model for the encapsidation of small DNA viruses.
format	article
author	Kimberly D Erickson Cedric Bouchet-Marquis Katie Heiser Eva Szomolanyi-Tsuda Rabinarayan Mishra Benjamin Lamothe Andreas Hoenger Robert L Garcea
author_facet	Kimberly D Erickson Cedric Bouchet-Marquis Katie Heiser Eva Szomolanyi-Tsuda Rabinarayan Mishra Benjamin Lamothe Andreas Hoenger Robert L Garcea
author_sort	Kimberly D Erickson
title	Virion assembly factories in the nucleus of polyomavirus-infected cells.
title_short	Virion assembly factories in the nucleus of polyomavirus-infected cells.
title_full	Virion assembly factories in the nucleus of polyomavirus-infected cells.
title_fullStr	Virion assembly factories in the nucleus of polyomavirus-infected cells.
title_full_unstemmed	Virion assembly factories in the nucleus of polyomavirus-infected cells.
title_sort	virion assembly factories in the nucleus of polyomavirus-infected cells.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/93985274bfbb4d58a415fc676e06b4ba
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Virion assembly factories in the nucleus of polyomavirus-infected cells.

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