The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.

The cellular endosomal sorting complex required for transport (ESCRT) machinery participates in membrane scission and cytoplasmic budding of many RNA viruses. Here, we found that expression of dominant negative ESCRT proteins caused a blockade of Epstein-Barr virus (EBV) release and retention of vir...

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Autores principales:	Chung-Pei Lee, Po-Ting Liu, Hsiu-Ni Kung, Mei-Tzu Su, Huey-Huey Chua, Yu-Hsin Chang, Chou-Wei Chang, Ching-Hwa Tsai, Fu-Tong Liu, Mei-Ru Chen
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/d7bef58ddf14482c855b9b7889ea4072
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spelling	oai:doaj.org-article:d7bef58ddf14482c855b9b7889ea40722021-11-18T06:03:59ZThe ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.1553-73661553-737410.1371/journal.ppat.1002904https://doaj.org/article/d7bef58ddf14482c855b9b7889ea40722012-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22969426/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The cellular endosomal sorting complex required for transport (ESCRT) machinery participates in membrane scission and cytoplasmic budding of many RNA viruses. Here, we found that expression of dominant negative ESCRT proteins caused a blockade of Epstein-Barr virus (EBV) release and retention of viral BFRF1 at the nuclear envelope. The ESCRT adaptor protein Alix was redistributed and partially colocalized with BFRF1 at the nuclear rim of virus replicating cells. Following transient transfection, BFRF1 associated with ESCRT proteins, reorganized the nuclear membrane and induced perinuclear vesicle formation. Multiple domains within BFRF1 mediated vesicle formation and Alix recruitment, whereas both Bro and PRR domains of Alix interacted with BFRF1. Inhibition of ESCRT machinery abolished BFRF1-induced vesicle formation, leading to the accumulation of viral DNA and capsid proteins in the nucleus of EBV-replicating cells. Overall, data here suggest that BFRF1 recruits the ESCRT components to modulate nuclear envelope for the nuclear egress of EBV.Chung-Pei LeePo-Ting LiuHsiu-Ni KungMei-Tzu SuHuey-Huey ChuaYu-Hsin ChangChou-Wei ChangChing-Hwa TsaiFu-Tong LiuMei-Ru ChenPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 9, p e1002904 (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 Chung-Pei Lee Po-Ting Liu Hsiu-Ni Kung Mei-Tzu Su Huey-Huey Chua Yu-Hsin Chang Chou-Wei Chang Ching-Hwa Tsai Fu-Tong Liu Mei-Ru Chen The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.
description	The cellular endosomal sorting complex required for transport (ESCRT) machinery participates in membrane scission and cytoplasmic budding of many RNA viruses. Here, we found that expression of dominant negative ESCRT proteins caused a blockade of Epstein-Barr virus (EBV) release and retention of viral BFRF1 at the nuclear envelope. The ESCRT adaptor protein Alix was redistributed and partially colocalized with BFRF1 at the nuclear rim of virus replicating cells. Following transient transfection, BFRF1 associated with ESCRT proteins, reorganized the nuclear membrane and induced perinuclear vesicle formation. Multiple domains within BFRF1 mediated vesicle formation and Alix recruitment, whereas both Bro and PRR domains of Alix interacted with BFRF1. Inhibition of ESCRT machinery abolished BFRF1-induced vesicle formation, leading to the accumulation of viral DNA and capsid proteins in the nucleus of EBV-replicating cells. Overall, data here suggest that BFRF1 recruits the ESCRT components to modulate nuclear envelope for the nuclear egress of EBV.
format	article
author	Chung-Pei Lee Po-Ting Liu Hsiu-Ni Kung Mei-Tzu Su Huey-Huey Chua Yu-Hsin Chang Chou-Wei Chang Ching-Hwa Tsai Fu-Tong Liu Mei-Ru Chen
author_facet	Chung-Pei Lee Po-Ting Liu Hsiu-Ni Kung Mei-Tzu Su Huey-Huey Chua Yu-Hsin Chang Chou-Wei Chang Ching-Hwa Tsai Fu-Tong Liu Mei-Ru Chen
author_sort	Chung-Pei Lee
title	The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.
title_short	The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.
title_full	The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.
title_fullStr	The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.
title_full_unstemmed	The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.
title_sort	escrt machinery is recruited by the viral bfrf1 protein to the nucleus-associated membrane for the maturation of epstein-barr virus.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/d7bef58ddf14482c855b9b7889ea4072
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The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus.

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