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Viroporins are a group of accessory proteins of interest as potential drug targets. Viroporins are small, highly hydrophobic, virus-encoded proteins that interact with cell membranes to alter the permeability of cells to ions or other small molecules. When these proteins oligomerize in the host cell membrane, they form hydrophilic pores that disrupt some of the physiological properties of the cell. They participate in the viral replication cycle by localizing on the membrane that connects the lumen of the ER to the cytoplasm. Viroporins are classified from I to III based on the number of their transmembrane domains. The positions of the amino- and carboxyl-terminal domains can be luminal or cytosolic, which determines their subsets.
Fig.1 Schematic representation of the pore formed by viroporins. (Gonzalez, 2003)
In general, their main function is to participate in the assembly of virions and their release from infected cells. Typically, deletion of a viral viroporin-coding gene from the viral genome greatly reduces viral progeny formation and viral pathogenicity, highlighting the essential role of these proteins in the viral life cycle. Viroporins are attractive targets for antiviral therapy because they are essential for viral release. In addition, their membrane osmotic activity may be inhibited in both artificial membranes and cell culture systems, thus facilitating the drug discovery process. Therefore, the use of classical viroporin inhibitors, as well as the development of new or highly specific drug derivatives, could enhance the efficacy of current antiviral therapies.
Modulation of ionic homeostasis within specific cellular compartments allows for viroporins to manipulate a wide range of cellular processes from autophagy, trafficking, inflammation, and transformation, to cell survival. Due to these broad perturbations to host cell physiology, viroporin function has been shown to assist in all stages of the virus life cycle including entry, membrane penetration, genome replication, and virus egress.
Transgene expression of viroporins in bacterial, yeast and mammalian cells facilitates analysis of their mode of action because their expression increases membrane permeability in all these cell types. Viroporin-induced membrane permeabilization to ions and/or small solutes can occur through the formation of gated channels or size-limited pores.
Many methods for studying the activity of viroporin are introduced.
The appearance of hemadsorption depends on the attachment of red blood cells (RBC) to the surface of cells infected with enveloped, hemagglutinin (HA) -producing viruses.
Test cells transfected with viroporin will have a pH shunt of these compartments, resulting in a diminished fluorescence signal. Fluorescence-based cellular assays were used for HCV p7 channels after recombinant expression on different cells. The assay can be applied to live cells or after fixing cells with paraformaldehyde.
This method has been used to determine viroporin activity (to reduce cell viability) and the function of viroporin inhibitors (to restore cell viability), and can also determine the cytotoxicity of potential viroporin inhibitors.
These methods allow direct study of viroporin channel behavior under similar conditions in vivo.
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