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Antiviral peptide targeting P protein oligomerization: proof of concept for mononegaviruses
Koyu Hara1, Nattika Nantachit2, Hiroshi Watanabe1
1Department of Infection Control and Prevention, Kurume University School of Medicine, Fukuoka, 830-0011, Japan.
Abstract:
In Mononegavirales, phosphoproteins (P) are essential polymerase cofactors, forming oligomers and interacting with viral components to facilitate replication. Previous studies have demonstrated that a P-derived peptide (PFr) from the respiratory syncytial virus (RSV), containing the oligomerization domain (OD) and C-terminal domain (CTD), effectively inhibits RSV replication. Here, we extend this approach to paramyxoviruses, including HPIV3, MeV and MuV. Customized PFrs exhibited potent inhibitory effects against their respective viruses, with IC50 values below 100 nM, while showing minimal cytotoxicity. These findings highlight the potential of targeting P oligomerization as a broad-spectrum antiviral strategy for paramyxoviruses and other mononegaviruses.
Insights
Researchers developed novel phosphoprotein-derived peptides (PFrs) that effectively inhibit paramyxovirus replication. This strategy targets viral polymerase cofactor oligomerization, showing broad-spectrum potential against related viruses.
Area of Science:
- Virology
- Molecular Biology
- Antiviral Drug Discovery
Background:
- Phosphoproteins (P) are crucial polymerase cofactors in Mononegavirales, essential for viral replication through oligomerization and interaction with viral components.
- Previous research showed that a respiratory syncytial virus (RSV) P-derived peptide (PFr) effectively inhibits RSV replication by targeting the P protein's oligomerization domain (OD) and C-terminal domain (CTD).
Purpose of the Study:
- To investigate the efficacy of P-derived peptides (PFrs) as an antiviral strategy against paramyxoviruses, including human parainfluenza virus type 3 (HPIV3), measles virus (MeV), and mumps virus (MuV).
- To evaluate the potential of targeting phosphoprotein oligomerization for broad-spectrum antiviral applications within the Mononegavirales order.
Main Methods:
- Design and synthesis of customized PFrs based on the P protein sequences of HPIV3, MeV, and MuV.
- In vitro antiviral assays to determine the inhibitory effects (IC50 values) of the synthesized PFrs against their respective viruses.
- Cytotoxicity assays to assess the safety profile of the PFrs.
Main Results:
- Customized PFrs demonstrated potent antiviral activity against HPIV3, MeV, and MuV, with half-maximal inhibitory concentration (IC50) values below 100 nM.
- The PFrs exhibited minimal cytotoxicity, indicating a favorable safety profile.
- The findings confirm the effectiveness of targeting P protein oligomerization for antiviral purposes in paramyxoviruses.
Conclusions:
- Targeting phosphoprotein oligomerization using P-derived peptides represents a promising antiviral strategy for paramyxoviruses.
- This approach holds potential for developing broad-spectrum antiviral therapeutics against a range of mononegaviruses.
