Nucleoprotein/NP Protein, H3N2 (P22435, sf9, His)

Nucleoprotein/NP Protein is vital for influenza virus replication and transcription.It binds to viral RNA, forming a ribonucleoprotein complex for genome replication.NP Protein interacts with host proteins, aiding viral pathogenesis and immune evasion.Understanding NP Protein's functions helps develop antiviral strategies against influenza.Nucleoprotein/NP Protein, H3N2 (P22435, sf9, His) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by Sf9 insect cells , with C-His labeled tag.

The Nucleoprotein (NP) encapsidates the negative strand viral RNA, safeguarding it against nucleases, and forms the ribonucleoprotein (RNP) complex that serves as a template for transcription and replication. To initiate an infectious cycle, the RNP needs to be localized in the host nucleus; however, it is too large to diffuse through the nuclear pore complex. NP contains at least 2 nuclear localization signals that actively facilitate RNP import into the nucleus via the cellular importin alpha/beta pathway. During later stages of infection, the nuclear export of RNPs is mediated by viral proteins NEP, which interact with M1, a protein that binds to nucleoproteins. NP may also directly bind to host exportin-1/XPO1, playing a crucial role in RNP nuclear export. The interaction between M1 and RNP conceals NP's nuclear localization signals. Following the infection of a new cell, M1 dissociates from the RNP due to acidification driven by M2 protein, uncovering NP's nuclear localization signals and allowing targeted RNP transport into the nucleus. Additionally, NP forms homomultimers to create the nucleocapsid and may bind to viral genomic RNA. Protein-RNA interactions involve a combination of electrostatic interactions between positively charged residues and the phosphate backbone, as well as planar interactions between aromatic side chains and bases.

Virus

Sf9 insect cells

C-His

P22435 (M1-N498)

/

Approximately 59.9 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.