As a member of the Flavivirus genus in the Flaviridae family, DV is a small, positive strand RNA enveloped virus. There are four serotypes of dengue virus (DV1-4). Their genome encodes a polyprotein precursor of at least seven non-structural proteins and three structural proteins which are the capsid protein (C), the membrane protein (M) and the envelope glycoprotein (E) [1] . The polyprotein is processed co-and post-translationally by cellular signalase in the lumen of the rough endoplasmic reticulum (ER) and by a viral protease in the cytosol [1, 2, 3] . The nascent C protein contains a C-terminal hydrophobic domain that acts as a signal sequence for translocation of the immature form of M, the prM, into the lumen of the rough ER. Two adjacent prM C-terminal transmembrane domains are responsible for prM membrane anchoring and E translocation into the ER [2] . prM and E associate into heterodimers at ER membranes [4, 5] where they assemble with the viral RNA/C complex to form progeny virions [1] . During the egress of virions through the secretory pathway, prM protein is cleaved by the trans-Golgi resident furin protease to form the M envelope protein and the soluble pr segment, which is released into the extracellular medium upon particle secretion [6] . prM cleavage marks maturation of flavivirus virions [7, 8] . Cleavage of prM is intimately correlated to change of conformation of envelope protein complexes. Although it was thought that prM cleavage is a prerequisite for E dimerization, recent studies show that change of conformation most probably occurs at low pH in the TGN and allows cleavage of prM by furin [6, 9, 10] .