Skip to Main content Skip to Navigation
Journal articles

A small fragmented P protein of respiratory syncytial virus inhibits virus infection by targeting P protein

Abstract : Peptide-based inhibitors hold promising potential in the development of antiviral therapy. Here, we investigated the antiviral potential of fragmented viral proteins derived from ribonucleoprotein (RNP) components of the human respiratory syncytial virus (HRSV). Based on a mimicking approach that targets the functional domains of viral proteins, we designed various fragments of nucleoprotein (N), matrix protein M2-1 and phosphoprotein (P) and tested the antiviral activity in an RSV mini-genome system. We found that the fragment comprising residues 130–180 and 212–241 in the C-terminal region of P (81 amino acid length), denoted as P Fr, significantly inhibited the polymerase activity through competitive binding to the full-length P. Further deletion analysis of P Fr suggested that three functional domains in P Fr (oligomerization, L-binding and nucleocapsid binding) are required for maximum inhibitory activity. More importantly, a purified recombinant P Fr displayed significant antiviral activity at low nanomolar range in RSV-infected HEp-2 cells. These results highlight P as an important target for the development of antiviral compounds against RSV and other paramyxoviruses.
Complete list of metadata

https://hal.inrae.fr/hal-03319367
Contributor : Camille Serva <>
Submitted on : Thursday, August 12, 2021 - 11:26:24 AM
Last modification on : Tuesday, August 17, 2021 - 6:03:51 PM

Links full text

Identifiers

Citation

Koyu Hara, Kenichiro Yaita, Pattara Khamrin, Kattareeya Kumthip, Takahito Kashiwagi, et al.. A small fragmented P protein of respiratory syncytial virus inhibits virus infection by targeting P protein. Journal of General Virology, Microbiology Society, 2020, 101 (1), pp.21-32. ⟨10.1099/jgv.0.001350⟩. ⟨hal-03319367⟩

Share

Metrics

Record views

20