ns2 , influenza

Non-structural protein 2 (NS2) plays a crucial role in the hepatitis C virus (HCV) assembly. NS2 was predicted to be composed of three transmembrane (TM) segments. Hepatitis C virus (HCV) nonstructural protein 2 (NS2) is a hydrophobic, transmembrane protein that is required not only for NS2-NS3 cleavage but also for infectious virus production.NS2 protein is essential for hepatitis C virus (HCV) replication. NS2 protein was expressed and purified. Aptamers against NS2 protein were raised and antiviral effects of the aptamers were examined. The non-structural protein NS2, also called nuclear export protein, of influenza A virus contains a leucine-rich nuclear export signal that could guide viral ribonucleoproteins to cross the nuclear pore complex (NPC) and complete directional nucleocytoplasmic trafficking.

Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.

Influenza A H3N2 (A/Aichi/2/1968) Hemagglutinin/HA Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 59 kDa and the accession number is P03437.1.

Influenza A H3N2 (A/Aichi/2/1968) Hemagglutinin/HA1 Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 37.6 kDa and the accession number is P03437.

Influenza A H7N9 (A Shanghai 2 2013) Nucleoprotein NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.8 kDa and the accession number is A0A024E372.

Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.

Influenza A H3N2 (A/Aichi/2/1968) Matrix protein 1/M1 Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 30 kDa and the accession number is I6SGW5.

Influenza A H3N2 (A/swine/Miyazaki/2/2013) Hemagglutinin/HA Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 57.7 kDa and the accession number is A0A077KEB1.

Influenza A H3N2 (A/Aichi/2/1968) Neuraminidase/NA Protein is expressed in HEK293 mammalian cells. The predicted molecular weight is 52.2 kDa and the accession number is Q75VQ4.1.

Influenza A H3N2 (A/Aichi/2/1968) Hemagglutinin/HA Protein (HA1+HA2, uncleaved) (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 59 kDa and the accession number is P03437.

Influenza A H7N9 (A/Shanghai/2/2013) Hemagglutinin/HA Protein (HEK293, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 57.6 kDa.

Influenza A H7N9 (A/Shanghai/2/2013) Hemagglutinin/HA Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.6 kDa.

Influenza A H3N2 (A/Aichi/2/1968) Nucleoprotein/NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.6 kDa and the accession number is I6TAH8.

Influenza A H3N2 (A/Aichi/2/1968) Neuraminidase/NA Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 50.8 kDa and the accession number is Q75VQ4.1.

The NS1 Influenza protein is created by the internal protein-encoding, linear negative-sense, single-stranded RNA, NS gene segment and which also codes for the nuclear export protein or NEP, formerly referred to as the NS2 protein, which mediates the export of vRNPs. The non-structural (NS1) protein is found in Influenzavirus A, Influenzavirus B, and Influenzavirus C. The non-structural (NS1) protein of the highly pathogenic avian H5N1 viruses circulating in poultry and waterfowl in Southeast Asia is currently believed to be responsible for the enhanced virulence of the strain. The Non-structural (NS1) protein of influenza A virus is a non-essential virulence factor that has multiple accessory functions during viral infection. The major role ascribed to NS1 has been its inhibition of host immune responses, especially the limitation of both interferon (IFN) production and the antiviral effects of IFN-induced proteins, such as dsRNA-dependent protein kinase R (PKR) and 2'5'-oligoadenylate synthetase (OAS)/RNase L. Non-structural (NS1) protein is a non-structural protein of the influenza A virus, which could only be expressed when cells are infected. The effect of NS1 protein on the host cell is still not clear. Not only could NS1 remarkably affect metabolism, but it could also slow down cell proliferation by blocking the cell cycle. Non-structural (NS1) protein may lead to the development of novel antiviral drugs, and the use of oncolytic influenza A viruses as potential anti-cancer agents.