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dc.contributor.authorKoyu Haraen_US
dc.contributor.authorKenichiro Yaitaen_US
dc.contributor.authorPattara Khamrinen_US
dc.contributor.authorKattareeya Kumthipen_US
dc.contributor.authorTakahito Kashiwagien_US
dc.contributor.authorJean François Eléouëten_US
dc.contributor.authorMarie Anne Rameix-Weltien_US
dc.contributor.authorHiroshi Watanabeen_US
dc.description.abstractPeptide-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.en_US
dc.subjectImmunology and Microbiologyen_US
dc.titleA small fragmented P protein of respiratory syncytial virus inhibits virus infection by targeting P proteinen_US
article.title.sourcetitleThe Journal of general virologyen_US
article.volume101en_USé de Virologie et Immunologie Moléculairesen_US de Versailles Saint-Quentin-en-Yvelinesen_US Ambroise Pare, Boulogne-Billancourten_US University School of Medicineen_US Mai Universityen_US General Hospitalen_US
Appears in Collections:CMUL: Journal Articles

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