Other influenza A H1N1 virion proteins

Other influenza A H1N1 virion proteins refers to a collective group of structural and functional proteins of the H1N1 influenza A virus, excluding the primary surface glycoproteins hemagglutinin and neuraminidase (ChEMBL CHEMBL2366514). This category encompasses the matrix proteins (M1 and M2), the nucleoprotein (NP), and the three subunits of the viral RNA-dependent RNA polymerase (RdRP) complex: polymerase acidic (PA), polymerase basic 1 (PB1), and polymerase basic 2 (PB2) (UniProt P03485, P03466, P03433). These proteins are essential for the viral life cycle, facilitating genome replication, transcription, viral assembly, and the evasion of host innate immunity (Wikipedia: Influenza A virus subtype H1N1). While hemagglutinin and neuraminidase are the traditional targets for vaccines and drugs, these internal proteins have become vital therapeutic targets to address the challenge of drug resistance (NIH: PMC6469017). For example, the PA subunit is targeted by the endonuclease inhibitor baloxavir marboxil, and the M2 ion channel is the target of adamantanes like amantadine (PubMed: 30189182). Because many of these internal proteins are highly conserved across different influenza strains, they are also the focus of research into universal influenza vaccines and broad-spectrum antivirals (StatPearls: Influenza). The nucleoprotein (NP) is another target of interest, as it is required for the encapsidation of the viral RNA segments (PubMed: 25410204). Non-structural proteins like NS1 play a key role in antagonizing the host interferon response, making them potential targets for immunomodulatory therapies (PubMed: 22438551).

Other names

H1N1 non-surface proteinsH1N1 internal proteinsInfluenza A virus (A/California/04/2009(H1N1)) proteinsH1N1 structural and non-structural proteins

Inhibition of the PA subunit cap-dependent endonuclease activity, blocking of the M2 proton channel to prevent viral uncoating, and inhibition of the RNA-dependent RNA polymerase (RdRP) complex.