FMDV nonstructural protein 2B contains two independent functional pores, both of which are essential for viral viability.
Should not yet guide FMDV antiviral development; leaves open therapeutic potential of dual-pore targeting pending natural-host validation.
FMDV nonstructural protein 2B is able to insert itself into cellular membranes to form a pore. This pore allows the passage of ions and small molecules through the membrane. In this study, we were able to show that both current and small molecules are able to pass though the pore made by 2B. We also discovered for the first time a virus with a pore-forming protein that contains two independent functional pores. By making mutations in our infectious clone of FMDV, we determined that mutations in either pore resulted in nonviable virus. This suggests that both pore-forming functions are independently required during FMDV infection.
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Gladue et al. (2018) studied this question.
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