Voltage-dependent anion channel 1 (VDAC1) (VDAC1)

Voltage-dependent anion channel 1 (VDAC1) has been identified as a key host cell surface receptor mediating the entry of Newcastle Disease Virus (NDV), including the highly virulent Italien strain (PubMed). While NDV initially attaches to sialic acid-containing glycoconjugates via its Hemagglutinin-Neuraminidase (HN) protein, the subsequent interaction with VDAC1 is crucial for viral internalisation and infection (PubMed). VDAC1 is a pore-forming protein primarily known for its role in the outer mitochondrial membrane, where it regulates the exchange of metabolites and ions between the mitochondria and the cytosol (UniProt). However, its presence on the plasma membrane allows it to serve as a gateway for certain viruses. The Italien strain, a velogenic form of NDV, causes severe respiratory and neurological disease in poultry, making the HN-VDAC1 interaction a significant target for antiviral development (NCBI). Experimental inhibitors like VBIT-4, which target VDAC1, have demonstrated the ability to block NDV entry, although the protein's essential role in cellular metabolism and apoptosis presents challenges for systemic therapeutic use (PubMed).

Other names

Outer mitochondrial membrane protein porin 1Plasmalemmal porinVDAC-1Sialic acid receptorNewcastle disease virus receptor

Inhibition of VDAC1 prevents its interaction with the viral Hemagglutinin-Neuraminidase (HN) protein, thereby blocking viral entry; alternatively, sialidases remove the primary attachment factor, sialic acid, to prevent viral binding.