The human polyoma JC virus agnoprotein acts as a viroporin.

Virus infections can result in a range of cellular injuries and commonly this involves both the plasma and intracellular membranes, resulting in enhanced permeability. Viroporins are a group of proteins that interact with plasma membranes modifying permeability and can promote the release of viral p...

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Autores principales:	Tadaki Suzuki, Yasuko Orba, Yuki Okada, Yuji Sunden, Takashi Kimura, Shinya Tanaka, Kazuo Nagashima, William W Hall, Hirofumi Sawa
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/5262113382964e2eb55c961001392d51
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spelling	oai:doaj.org-article:5262113382964e2eb55c961001392d512021-11-25T05:48:14ZThe human polyoma JC virus agnoprotein acts as a viroporin.1553-73661553-737410.1371/journal.ppat.1000801https://doaj.org/article/5262113382964e2eb55c961001392d512010-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20300659/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Virus infections can result in a range of cellular injuries and commonly this involves both the plasma and intracellular membranes, resulting in enhanced permeability. Viroporins are a group of proteins that interact with plasma membranes modifying permeability and can promote the release of viral particles. While these proteins are not essential for virus replication, their activity certainly promotes virus growth. Progressive multifocal leukoencephalopathy (PML) is a fatal demyelinating disease resulting from lytic infection of oligodendrocytes by the polyomavirus JC virus (JCV). The genome of JCV encodes six major proteins including a small auxiliary protein known as agnoprotein. Studies on other polyomavirus agnoproteins have suggested that the protein may contribute to viral propagation at various stages in the replication cycle, including transcription, translation, processing of late viral proteins, assembly of virions, and viral propagation. Previous studies from our and other laboratories have indicated that JCV agnoprotein plays an important, although as yet incompletely understood role in the propagation of JCV. Here, we demonstrate that agnoprotein possesses properties commonly associated with viroporins. Our findings demonstrate that: (i) A deletion mutant of agnoprotein is defective in virion release and viral propagation; (ii) Agnoprotein localizes to the ER early in infection, but is also found at the plasma membrane late in infection; (iii) Agnoprotein is an integral membrane protein and forms homo-oligomers; (iv) Agnoprotein enhances permeability of cells to the translation inhibitor hygromycin B; (v) Agnoprotein induces the influx of extracellular Ca(2+); (vi) The basic residues at amino acid positions 8 and 9 of agnoprotein key are determinants of the viroporin activity. The viroporin-like properties of agnoprotein result in increased membrane permeability and alterations in intracellular Ca(2+) homeostasis leading to membrane dysfunction and enhancement of virus release.Tadaki SuzukiYasuko OrbaYuki OkadaYuji SundenTakashi KimuraShinya TanakaKazuo NagashimaWilliam W HallHirofumi SawaPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 6, Iss 3, p e1000801 (2010)
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 Tadaki Suzuki Yasuko Orba Yuki Okada Yuji Sunden Takashi Kimura Shinya Tanaka Kazuo Nagashima William W Hall Hirofumi Sawa The human polyoma JC virus agnoprotein acts as a viroporin.
description	Virus infections can result in a range of cellular injuries and commonly this involves both the plasma and intracellular membranes, resulting in enhanced permeability. Viroporins are a group of proteins that interact with plasma membranes modifying permeability and can promote the release of viral particles. While these proteins are not essential for virus replication, their activity certainly promotes virus growth. Progressive multifocal leukoencephalopathy (PML) is a fatal demyelinating disease resulting from lytic infection of oligodendrocytes by the polyomavirus JC virus (JCV). The genome of JCV encodes six major proteins including a small auxiliary protein known as agnoprotein. Studies on other polyomavirus agnoproteins have suggested that the protein may contribute to viral propagation at various stages in the replication cycle, including transcription, translation, processing of late viral proteins, assembly of virions, and viral propagation. Previous studies from our and other laboratories have indicated that JCV agnoprotein plays an important, although as yet incompletely understood role in the propagation of JCV. Here, we demonstrate that agnoprotein possesses properties commonly associated with viroporins. Our findings demonstrate that: (i) A deletion mutant of agnoprotein is defective in virion release and viral propagation; (ii) Agnoprotein localizes to the ER early in infection, but is also found at the plasma membrane late in infection; (iii) Agnoprotein is an integral membrane protein and forms homo-oligomers; (iv) Agnoprotein enhances permeability of cells to the translation inhibitor hygromycin B; (v) Agnoprotein induces the influx of extracellular Ca(2+); (vi) The basic residues at amino acid positions 8 and 9 of agnoprotein key are determinants of the viroporin activity. The viroporin-like properties of agnoprotein result in increased membrane permeability and alterations in intracellular Ca(2+) homeostasis leading to membrane dysfunction and enhancement of virus release.
format	article
author	Tadaki Suzuki Yasuko Orba Yuki Okada Yuji Sunden Takashi Kimura Shinya Tanaka Kazuo Nagashima William W Hall Hirofumi Sawa
author_facet	Tadaki Suzuki Yasuko Orba Yuki Okada Yuji Sunden Takashi Kimura Shinya Tanaka Kazuo Nagashima William W Hall Hirofumi Sawa
author_sort	Tadaki Suzuki
title	The human polyoma JC virus agnoprotein acts as a viroporin.
title_short	The human polyoma JC virus agnoprotein acts as a viroporin.
title_full	The human polyoma JC virus agnoprotein acts as a viroporin.
title_fullStr	The human polyoma JC virus agnoprotein acts as a viroporin.
title_full_unstemmed	The human polyoma JC virus agnoprotein acts as a viroporin.
title_sort	human polyoma jc virus agnoprotein acts as a viroporin.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/5262113382964e2eb55c961001392d51
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The human polyoma JC virus agnoprotein acts as a viroporin.

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