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• W4361851718 startingPage "1834" @default.
• W4361851718 abstract "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." @default.
• W4361851718 created "2023-04-05" @default.
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• W4361851718 date "2008-03-28" @default.
• W4361851718 modified "2023-10-11" @default.
• W4361851718 title "Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation" @default.
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• W4361851718 doi "https://doi.org/10.1126/science.1153264" @default.
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