Vironova’s antiviral approach is to stop viral growth by inhibiting viral structures from forming, e.g. the capsid. Correct assembly of structural proteins is essential for the virus to survive the extracellular environment and to become infectious, and is thus a suitable drug target.
This novel class of antivirals is particularly promising for three reasons:
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The targets are protein-protein contacts between the virus structural proteins, which are crucial for correct assembly of the virus into infectious virions.
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The protein domain that is targeted is often highly conserved among different viruses within the same family which enables broad range treatment.
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They inhibit essential protein-protein interactions between virus structural proteins that are critical for the overall integrity and survival of the virus particle, to which drug-induced mutations would lead to non-infectious virus particles.
Vironova is unique in its antiviral strategy since there has been a lack in tools to evaluate such substances. Vironova’s image analysis technology allows a very detailed analysis of the mechanism of action of structural inhibitors.
Illustration of virus capsid assembly
Virus capsid assembly is commonly a stepwise intracellular process. It usually starts with proteins (A) that assemble into larger building blocks (B), which then assemble into virus capsids (C). Most virus capsids are symmetrical and are made up of 60 identical protein units. This means that there are a certain number contacts between the proteins that are needed to maintain the virus particle. These contacts are both within and between the protein building blocks. Vironova’s antiviral strategy is to inhibit these protein-protein contacts, which are essential for the virus to form its protective shield and become infectious.