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The Human Polyoma JC Virus Agnoprotein Acts as a Viroporin

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Title: The Human Polyoma JC Virus Agnoprotein Acts as a Viroporin
Authors: Suzuki, Tadaki Browse this author
Orba, Yasuko Browse this author
Okada, Yuki Browse this author
Sunden, Yuji Browse this author
Kimura, Takashi Browse this author
Tanaka, Shinya Browse this author →KAKEN DB
Nagashima, Kazuo Browse this author
Hall, William W. Browse this author
Sawa, Hirofumi Browse this author
Issue Date: 12-Mar-2010
Publisher: Public Library of Science
Journal Title: PLoS Pathogens
Volume: 6
Issue: 3
Start Page: e1000801
Publisher DOI: 10.1371/journal.ppat.1000801
Abstract: 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 Ca2+; (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 Ca2+ homeostasis leading to membrane dysfunction and enhancement of virus release.
Rights: http://creativecommons.org/licenses/by/2.5/
Type: article
URI: http://hdl.handle.net/2115/43091
Appears in Collections:人獣共通感染症リサーチセンター (Research Center for Zoonosis Control) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 澤 洋文

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