Recombinant Japanese encephalitis virus NS1 glycoprotein (His tag) is a Japanese encephalitis virus strain SA-14 Full Length protein, in the 795 to 1146 aa range, expressed in HEK 293, with >95% purity and suitable for SDS-PAGE.
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| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Capsid protein C. 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. Capsid protein C. Inhibits RNA silencing by interfering with host Dicer. Peptide pr. Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. 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 peptide. 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. Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HSPA5 (PubMed:28053106). 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 heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. 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 2A. Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response. Serine protease subunit NS2B. Required cofactor for the serine protease function of NS3 (PubMed:7897348). May have membrane-destabilizing activity and form viroporins (By similarity). Serine protease NS3. Displays three enzymatic activities: serine protease, NTPase and RNA helicase (PubMed:18201743, PubMed:7897348). 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 (Probable). NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Non-structural protein 4A. Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (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 (By similarity). 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 (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity). RNA-directed RNA polymerase NS5. Replicates the viral (+) and (-) RNA genome (PubMed:24293643). Performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (By similarity). 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:16731929). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16731929).
Japanese encephalitis virus NS1 glycoprotein
Genome polyprotein
Recombinant Japanese encephalitis virus NS1 glycoprotein (His tag) is a Japanese encephalitis virus strain SA-14 Full Length protein, in the 795 to 1146 aa range, expressed in HEK 293, with >95% purity and suitable for SDS-PAGE.
pH: 7 - 8
Constituents: 100% PBS
ab218555 was 0.2 um filter sterilised.
Capsid protein C
In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.
Genome polyprotein
The antigen is in its native folding state, and possesses all post-translational modifications. Unlike other flavivirus NS1 proteins which secrete as a single hexameric form, Japanese Encephalitis virus NS1 shows two oligomeric states in approximately equal proportion.
The Japanese encephalitis virus NS1 glycoprotein also known as NS1 is an important non-structural protein in the lifecycle of the Japanese encephalitis virus. It has a molecular mass of approximately 46 kDa and is expressed in both the infected host cells and the virus itself. NS1 plays an important role in viral replication and immune evasion making it a significant focus of research. It is expressed on the surface of infected cells as a dimer or can be secreted as a hexamer providing multiple functional roles and making it a target for antibody development.
The NS1 glycoprotein participates in the virus's evasion of the host's immune system. It doesn't operate as part of a complex but serves several independent functions. NS1 helps inhibit the host's complement system reducing the immune-mediated damage to the virus-infected cells. Additionally it assists in viral RNA synthesis by enhancing the efficiency of the viral replication complex supporting the production of new viral particles within the infected cell environment.
The NS1 glycoprotein interacts with several host cell mechanisms to modulate the immune response. Specifically it is involved in the complement inhibition and RNA synthesis pathways. In the complement inhibition pathway NS1 plays a part by binding to host complement proteins impeding their function and providing an advantage to the virus against the host immune defense. Its association with the viral RNA synthesis pathway is essential for the replication of the Japanese encephalitis virus coordinating with other non-structural proteins like NS3 to ensure effective viral proliferation.
NS1 is closely linked to the pathogenesis of Japanese encephalitis and other flavivirus-related conditions. The protein's interaction with host immune responses directly correlates with the severity of these diseases by contributing to immune evasion and facilitating virus spread within the host. Additionally NS1 has been observed to share functional similarities with proteins of other viruses including dengue virus NS1 which plays a similar role in disrupting immune pathways and aiding in viral replication. Understanding these connections helps in developing effective strategies for therapeutic interventions against flaviviruses.
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