Recombinant Dengue Virus 2 NS1 glycoprotein (6x His tag C-Terminus)

Specifications

Form

Liquid

General info

Function

Capsid protein C. Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed : 23522008).. Peptide pr. Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.. Protein prM. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion loop. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.. Small envelope protein M. May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.. Envelope protein E. Type II fusion protein that binds to host cell surface receptor and mediates fusion between viral and cellular membranes (Probable). The envelope protein E shifts from dimeric state to trimeric state to perform fusion with the host membrane (By similarity). The fusion loops of the three subunits come together to form a membrane-insertable tip containing aromatic residues (By similarity). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers of precursor prM and envelope protein E (By similarity). Envelope protein exposes a positively-charged pr-binding pocket at the E dimer interface, inducing (prM/E)2 dimer formation to generate smooth particles in the Golgi (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion (By similarity). Pr is shed from the particle upon subsequent secretion into the extracellular environment, leaving an activated particle, prone to mediate acidic pH-triggered membrane fusion upon entry into a target cell (By similarity).. Non-structural protein 1. Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations : the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).. Non-structural protein 1. Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations : the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3) (By similarity). Mediates complement activation, which may contribute to the pathogenesis of the vascular leakage that occurs in severe dengue disease (PubMed : 16544248). Activates autophagy through the AMPK/ERK/mTOR signaling pathway. Mechanistically, acts as the assembly platform for STK11-AMPK interactions and promotes STK11-AMPK interactions. In turn, promotes phosphorylation of the AMPK kinase structural domain and activates AMPK, thereby positively regulating the AMPK/ERK/mTOR signaling pathway and inducing autophagy (PubMed : 37821951).. Non-structural protein 2A. Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.. Serine protease subunit NS2B. Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).. Serine protease NS3. Displays three enzymatic activities : serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm : C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.. Non-structural protein 4A. Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between RIGI and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity).. Peptide 2k. Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.. Non-structural protein 4B. Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (PubMed : 15956546).. RNA-directed RNA polymerase/Methyltransferase NS5. Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed : 19850911). Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed : 15944325). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed : 19754307). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (PubMed : 30550790).

Sequence similarities

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.

Post-translational modifications

Genome polyprotein. Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.. Protein prM. Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.. Envelope protein E. N-glycosylated.. Non-structural protein 1. N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.. Serine protease NS3. Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication.. RNA-directed RNA polymerase/Methyltransferase NS5. Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.. RNA-directed RNA polymerase/Methyltransferase NS5. Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.