Influenza virus NS1A-binding protein (IVNS1ABP)

Influenza virus NS1A-binding protein (IVNS1ABP) is a multifunctional human protein that acts as an adaptor and regulator for protein and RNA complexes, notably interacting with influenza A virus non-structural protein 1 (NS1)[1][2]. It regulates several cellular processes, including pre-mRNA splicing (promoting alternative and viral mRNA splicing), mRNA nuclear export, and actin filament stabilization. Its BTB and Kelch domains mediate dimerization and facilitate binding to splicing machinery and cytoskeletal components[1]. IVNS1ABP plays an essential role in facilitating efficient viral gene expression, viral replication, and suppression of apoptosis during influenza A infection, while also participating in the negative regulation of protein ubiquitination and modulating the aryl hydrocarbon receptor pathway. It is implicated in human disease as a host factor in viral infections and in rare cases of primary immunodeficiency (Immunodeficiency 70)[1][2][3]. No drugs are currently known to directly target IVNS1ABP, nor are biomarkers or established mechanisms of action for drug targeting documented. The molecule is not a classic therapeutic target (e.g., receptor, enzyme) but is of interest as a host cofactor in infection biology[1][2].

Other names

ARA3FLARA3HSPC068KIAA0850KLHL39ND1NS-1NS1-BPNS1BPIMD70Aryl hydrocarbon receptor-associated protein 3Kelch-like family member 39NCX downstream gene 1