HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
人獣共通感染症リサーチセンター  >
雑誌発表論文等  >

The Human Polyoma JC Virus Agnoprotein Acts as a Viroporin


PP6-3_e1000801.pdf2.57 MBPDF見る/開く

タイトル: The Human Polyoma JC Virus Agnoprotein Acts as a Viroporin
著者: Suzuki, Tadaki 著作を一覧する
Orba, Yasuko 著作を一覧する
Okada, Yuki 著作を一覧する
Sunden, Yuji 著作を一覧する
Kimura, Takashi 著作を一覧する
Tanaka, Shinya 著作を一覧する
Nagashima, Kazuo 著作を一覧する
Hall, William W. 著作を一覧する
Sawa, Hirofumi 著作を一覧する
発行日: 2010年 3月12日
出版者: Public Library of Science
誌名: PLoS Pathogens
巻: 6
号: 3
開始ページ: e1000801
出版社 DOI: 10.1371/journal.ppat.1000801
抄録: 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.
資料タイプ: article
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 澤 洋文


本サイトに関するご意見・お問い合わせは repo at へお願いします。 - 北海道大学