3C6R

Low pH Immature Dengue Virus

Summary for 3C6R

• Entry DOI: 10.2210/pdb3c6r/pdb
• EMDB information: 5006
• Descriptor: Envelope protein, Peptide pr (2 entities in total)
• Functional Keywords: 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, virus
• Biological source: Dengue virus type 2; More
• Total number of polymer chains: 6
• Total formula weight: 159497.82

Authors

Yu, I.,Zhang, W.,Holdway, H.A.,Li, L.,Kostyuchenko, V.A.,Chipman, P.R.,Kuhn, R.J.,Rossmann, M.G.,Chen, J. (deposition date: 2008-02-05, release date: 2008-04-22, Last modification date: 2024-02-21)

Primary citation

Yu, I.M.,Zhang, W.,Holdaway, H.A.,Li, L.,Kostyuchenko, V.A.,Chipman, P.R.,Kuhn, R.J.,Rossmann, M.G.,Chen, J.
Structure of the immature dengue virus at low pH primes proteolytic maturation
Science, 319:1834-1837, 2008

PubMed 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.

PubMed: 18369148
DOI: 10.1126/science.1153264

Experimental method

ELECTRON MICROSCOPY (25 Å)