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© Research
Publication : The Journal of general virology

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of general virology - 01 Jan 2020

Hara K, Yaita K, Khamrin P, Kumthip K, Kashiwagi T, Eléouët JF, Rameix-Welti MA, Watanabe H,

Link to Pubmed [PMID] – 31702536

Link to DOI – 10.1099/jgv.0.001350

J Gen Virol 2020 Jan; 101(1): 21-32

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.

https://pubmed.ncbi.nlm.nih.gov/31702536