Matusevich OV, Egorov VV, Gluzdikov IA, Titov MI, Zarubaev VV, Shtro AA, Slita AV, Dukov MI, Shurygina AP, Smirnova TD, Kudryavtsev IV, Vasin AV, Kiselev OI.
- Antiviral Research , 2015
This study is devoted to the antiviral activity of peptide fragments from the PB1 protein – a component of the influenza A RNA polymerase. The antiviral activity of the peptides synthesized was studied in MDCK cell cultures against the pandemic influenza strain A/California/07/2009 (H1N1) pdm09. We ...
This study is devoted to the antiviral activity of peptide fragments from the PB1 protein – a component of the influenza A RNA polymerase. The antiviral activity of the peptides synthesized was studied in MDCK cell cultures against the pandemic influenza strain A/California/07/2009 (H1N1) pdm09. We found that peptide fragments 6-13, 6-14, 26-30, 395-400, and 531-540 of the PB1 protein were capable of suppressing viral replication in cell culture. Terminal modifications i.e. N-acetylation and C-amidation increased the antiviral properties of the peptides significantly. Peptide PB1 (6 – 14) with both termini modified showed maximum antiviral activity, its inhibitory activity manifesting itself during the early stages of viral replication. It was also shown that the fluorescent-labeled analog of this peptide was able to penetrate into the cell. The broad range of virus-inhibiting activity of PB1 (6-14) peptide was confirmed using a panel of influenza A viruses of H1, H3 and H5 subtypes including those resistant to oseltamivir, the leading drug in anti-influenza therapy. Thus, short peptide fragments of the PB1 protein could serve as leads for future development of influenza prevention and/or treatment agents.
Antiviral Research 2015 Jan;113:4-10. doi: 10.1016/j.antiviral.2014.10.015. Epub 2014 Nov 12
