Recombinant Hepatitis GB virus B Genome polyprotein, partial

Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A. Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication. Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit. Probably affects various cell signaling pathways, host immunity and lipid metabolism (Probable).; Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism.; Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism.; May function as a multimeric ion channel protein (viroporin).; Cysteine protease required for the proteolytic auto-cleavage between the non-structural proteins NS2 and NS3. The N-terminus of NS3 is required for the function of NS2 protease (active region NS2-3). Promotes the initiation of viral particle assembly by mediating the interaction between structural and non-structural proteins.; Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and likely resolves RNA complicated stable secondary structures in the template strand. Cleaves host MAVS/CARDIF thereby preventing the establishment of an antiviral state.; Induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex. NS4B self-interaction contributes to its function in membranous web formation.; Phosphorylated protein that is indispensable for viral replication and assembly.; RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication.