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Antiviral Res. 2015 Jan;113:4-10. doi: 10.1016/j.antiviral.2014.10.015. Epub 2014 Nov 12.

Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments.

Author information

1
Saint Petersburg State University, Faculty of Chemistry, 26, Universitetskii pr., Petrodvorets, St. Petersburg 198504, Russia.
2
Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., St. Petersburg 197376, Russia; Petersburg Nuclear Physics Institute, NRC KI, Orlova roscha, Gatchina 188300, Russia. Electronic address: toizeg@gmail.com.
3
Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., St. Petersburg 197376, Russia.
4
Institute of Experimental Medicine of the North-West Branch of the Russian Academy of Medical Sciences (IEM NWB RAMS), 12, Akad. Pavlova str., St. Petersburg 197376, Russia; Far East Federal University, 8, Suhanova str., Vladivostok 690950, Russia.
5
Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., St. Petersburg 197376, Russia; State Polytechnical University, 29, Polytecnicheskaya str., St. Petersburg 195251, Russia.

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.

KEYWORDS:

Antiviral peptides; Influenza A; Influenza A polymerase; PB1

PMID:
25446335
DOI:
10.1016/j.antiviral.2014.10.015
[Indexed for MEDLINE]

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