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Dengue Virus Life Cycle

Dengue Virus Life Cycle

Dengue virus exists as a number of different viral forms depending on the degree of precursor membrane (prM) protein cleavage. Fully immature dengue virus particles contain a full complement of prM proteins and are non-infectious, whereas all prM proteins are cleaved in fully mature virus particles. A number of intermediate, partially mature forms exist in which some prM proteins have been cleaved and some remain intact. Fully mature and some of the partially mature virus particles are infectious (step 1). The dengue viral replication process begins when a virion attaches directly to a diverse group of host cell receptors or when the Fc portion of a dengue virus-containing immune complex attaches to a Fc receptor on the target cells (step 2) and subsequently enters the cell by receptor-mediated endocytosis (step 3). Acidification of the endosomal vesicles triggers conformational changes in the virion, resulting in an irreversible trimerization of the viral envelope (E) protein (not shown). This exposes the fusion peptide and mediates fusion between the viral and the endosomal membranes, allowing the release of the nucleocapsid into the cytoplasm. The viral RNA is released into the cytoplasm and presented to the rough endoplasmic reticulum (ER) (step 4). At the ER, viral RNA is translated into a single polyprotein that is processed by viral and host proteases (step 5). After the viral replication complex is synthesized, viral RNA translation switches off, and RNA synthesis begins by the transcription of an antisense viral RNA followed by the amplification of viral RNA (step 6). The newly synthesized RNA is subsequently packaged by capsid (C) protein, forming a nucleocapsid (step 7). Virus assembly occurs on the surface of the ER when the nucleocapsid buds into the ER lumen, resulting in non-infectious, immature viral particles (step 8). Immature viral particles are transported through the Golgi into the trans-Golgi network, where acidification induces conformational changes of the virion and exposes the furin cleavage sites. The host protease furin cleaves between pr protein and M protein, with the pr protein remaining associated until the virion is released in the neutral pH of the extracellular millieu (step 9). DC-SIGN, dendritic cell-specific ICAM3-grabbing non-integrin; NS proteins, non-structural proteins.
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