Flavivirus

Structure and dynamics of the monomer of protein E of dengue virus type 2 with unprotonated histidine residues

L. Degrève and Fuzo, C. A., Structure and dynamics of the monomer of protein E of dengue virus type 2 with unprotonated histidine residues, vol. 12, pp. 348-359, 2013.

The surface of the dengue virus is composed of 180 copies of a multifunctional envelope glycoprotein that acts at several stages of viral infection. When the virus is in the endosome, these glycoproteins undergo major conformational rearrangements owing to the protonation of histidine side chains. This protonation allows for the formation of trimers, thereby triggering fusion between the viral and the host membranes.

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