3IYA

Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH

3IYA の概要

• エントリーDOI: 10.2210/pdb3iya/pdb
• EMDBエントリー: 5117
• 分子名称: Envelope protein, prM protein (2 entities in total)
• 機能のキーワード: prm, e, icosahedral virus, virus
• 由来する生物種: Dengue virus 2; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 159497.82

構造登録者

Yu, I.,Holdaway, H.A.,Chipman, P.R.,Kuhn, R.J.,Rossmann, M.G.,Chen, J. (登録日: 2009-06-01, 公開日: 2010-04-14, 最終更新日: 2024-02-21)

主引用文献

Yu, I.M.,Holdaway, H.A.,Chipman, P.R.,Kuhn, R.J.,Rossmann, M.G.,Chen, J.
Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion.
J.Virol., 83:12101-12107, 2009

PubMed Abstract: Flavivirus assembles into an inert particle that requires proteolytic activation by furin to enable transmission to other hosts. We previously showed that immature virus undergoes a conformational change at low pH that renders it accessible to furin (I. M. Yu, W. Zhang, H. A. Holdaway, L. Li, V. A. Kostyuchenko, P. R. Chipman, R. J. Kuhn, M. G. Rossmann, and J. Chen, Science 319:1834-1837, 2008). Here we show, using cryoelectron microscopy, that the structure of immature dengue virus at pH 6.0 is essentially the same before and after the cleavage of prM. The structure shows that after cleavage, the proteolytic product pr remains associated with the virion at acidic pH, and that furin cleavage by itself does not induce any major conformational changes. We also show by liposome cofloatation experiments that pr retention prevents membrane insertion, suggesting that pr is present on the virion in the trans-Golgi network to protect the progeny virus from fusion within the host cell.

PubMed: 19759134
DOI: 10.1128/JVI.01637-09

実験手法

ELECTRON MICROSCOPY (22 Å)