tetano
Editor, Senior Moderator
Antiviral Res. 2014 Nov 12;113C:4-10. doi: 10.1016/j.antiviral.2014.10.015. [Epub ahead of print]
Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments.
Matusevich OV1, Egorov VV2, Gluzdikov IA1, Titov MI1, Zarubaev VV3, Shtro AA3, Slita AV3, Dukov MI3, Shurygina AP3, Smirnova TD3, Kudryavtsev IV4, Vasin AV5, Kiselev OI3.
Author information
Abstract
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.
Copyright ? 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
Antiviral peptides; Influenza A; Influenza A polymerase; PB1
PMID:
25446335
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25446335
Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments.
Matusevich OV1, Egorov VV2, Gluzdikov IA1, Titov MI1, Zarubaev VV3, Shtro AA3, Slita AV3, Dukov MI3, Shurygina AP3, Smirnova TD3, Kudryavtsev IV4, Vasin AV5, Kiselev OI3.
Author information
Abstract
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.
Copyright ? 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
Antiviral peptides; Influenza A; Influenza A polymerase; PB1
PMID:
25446335
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25446335