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-Structure paper
タイトル | Structure of the immature dengue virus at low pH primes proteolytic maturation. |
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ジャーナル・号・ページ | Science, Vol. 319, Issue 5871, Page 1834-1837, Year 2008 |
掲載日 | 2008年3月28日 |
著者 | I-Mei Yu / Wei Zhang / Heather A Holdaway / Long Li / Victor A Kostyuchenko / Paul R Chipman / Richard J Kuhn / Michael G Rossmann / Jue Chen / |
PubMed 要旨 | Intracellular cleavage of immature flaviviruses is a critical step in assembly that generates the membrane fusion potential of the E glycoprotein. With cryo-electron microscopy we show that the ...Intracellular cleavage of immature flaviviruses is a critical step in assembly that generates the membrane fusion potential of the E glycoprotein. With cryo-electron microscopy we show that the immature dengue particles undergo a reversible conformational change at low pH that renders them accessible to furin cleavage. At a pH of 6.0, the E proteins are arranged in a herringbone pattern with the pr peptides docked onto the fusion loops, a configuration similar to that of the mature virion. After cleavage, the dissociation of pr is pH-dependent, suggesting that in the acidic environment of the trans-Golgi network pr is retained on the virion to prevent membrane fusion. These results suggest a mechanism by which flaviviruses are processed and stabilized in the host cell secretory pathway. |
リンク | Science / PubMed:18369148 |
手法 | EM (単粒子) |
解像度 | 25.0 Å |
構造データ | |
由来 |
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キーワード | VIRUS / dengue / immature / prM / E / Capsid protein / Cleavage on pair of basic residues / Core protein / Endoplasmic reticulum / Envelope protein / Glycoprotein / Membrane / Secreted / Transmembrane / Virion / icosahedral virus |