Recombinant Hantavirus Dobrava, strain Slovenia, nucleocapsid protein is a Dobrava-Belgrade orthohantavirus Full Length protein, expressed in Saccharomyces cerevisiae, with >95% purity and suitable for SDS-PAGE, ELISA, WB.
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info 2 µg/mL | Notes - |
Application ELISA | Reactivity Reacts | Dilution info 2 µg/mL | Notes - |
Application WB | Reactivity Reacts | Dilution info 1.00000-2.00000 µg/mL | Notes - |
Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity).
Nucleoprotein, Nucleocapsid protein, Protein N
Recombinant Hantavirus Dobrava, strain Slovenia, nucleocapsid protein is a Dobrava-Belgrade orthohantavirus Full Length protein, expressed in Saccharomyces cerevisiae, with >95% purity and suitable for SDS-PAGE, ELISA, WB.
Constituents: PBS
Purified by chromatography under denaturing conditions.
Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity).
Belongs to the hantavirus nucleocapsid protein family.
The Hantavirus Dobrava strain Slovenia nucleocapsid protein also called N protein plays an important role in viral replication and assembly. This protein has a mass of approximately 50 kDa and is integral for encapsidating the viral RNA genome. It mainly expresses in infected host cells forming the basis of the ribonucleoprotein complex that is fundamental for the virus life cycle. The nucleocapsid protein serves as a scaffold for the construction of the viral capsid facilitating interactions with host cells' machinery.
This nucleocapsid protein is involved in several critical processes for the virus. It forms part of a larger complex the ribonucleoprotein complex which includes the viral RNA and other key proteins. This complex serves as the template for replication and transcription of the viral genome ensuring the production of new viral particles. The N protein's ability to bind RNA and other nucleocapsid proteins makes it central to the regulation of these processes. Understanding its role provides insights into how hantaviruses hijack host cells for replication.
The nucleocapsid protein from the Dobrava hantavirus strain participates in significant pathways related to viral replication and innate immune response evasion. It interacts with pathways involving the RIG-I-like receptor signaling helping the virus avoid detection by the host's immune system. Proteins such as RIG-I and MDA5 play a role here as they typically detect viral RNA but are often inhibited by this viral protein's functions allowing the virus to replicate undetected initially.
The nucleocapsid protein of the Dobrava hantavirus strain contributes to hemorrhagic fever with renal syndrome (HFRS) a severe disease caused by hantavirus infections. Its interaction with proteins such as interferon regulatory factors (IRFs) demonstrates its role in modulating immune responses exacerbating disease progression. Understanding the nucleocapsid's interactions and functions helps in identifying therapeutic targets to mitigate the effects of hantavirus-related diseases.
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SDS-PAGE showing ab74556 at approximately 50kDa. (2 μg/lane).
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