@ARTICLE{Matusevich20154,
author={Matusevich, O.V. and Egorov, V.V. and Gluzdikov, I.A. and Titov, M.I. and Zarubaev, V.V. and Shtro, A.A. and Slita, A.V. and Dukov, M.I. and Shurygina, A.-P.S. and Smirnova, T.D. and Kudryavtsev, I.V. and Vasin, A.V. and Kiselev, O.I.},
title={Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments},
journal={Antiviral Research},
year={2015},
volume={113},
pages={4-10},
doi={10.1016/j.antiviral.2014.10.015},
note={cited By 6},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84911884647&doi=10.1016%2fj.antiviral.2014.10.015&partnerID=40&md5=ee11406f9aea9680cc6c4c4cec4df9af},
affiliation={Saint Petersburg State University, Faculty of Chemistry, 26, Universitetskii pr., Petrodvorets, St.-Petersburg, 198504, Russian Federation; Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., St.-Petersburg, 197376, Russian Federation; Inst. of Experimental Medicine of the North-West Branch of the Russian Academy of Medical Sciences, 12, Akad. Pavlova str., St.-Petersburg, 197376, Russian Federation; Petersburg Nuclear Physics Institute, NRC KI, Orlova roscha, Gatchina, 188300, Russian Federation; Far East Federal University, 8, Suhanova str., Vladivostok, 690950, Russian Federation; State Polytechnical University, 29, Polytecnicheskaya str., St.-Petersburg, 195251, Russian Federation},
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. © 2014 Elsevier B.V. All rights reserved.},
author_keywords={Antiviral peptides;  Influenza A;  Influenza A polymerase;  PB1},
correspondence_address1={Egorov, V.V.; Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., Russian Federation},
publisher={Elsevier B.V.},
issn={01663542},
coden={ARSRD},
pubmed_id={25446335},
language={English},
abbrev_source_title={Antiviral Res.},
document_type={Article},
source={Scopus},
}

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Pavlova str., St.-Petersburg, 197376, Russian Federation; Petersburg Nuclear Physics Institute, NRC KI, Orlova roscha, Gatchina, 188300, Russian Federation; Far East Federal University, 8, Suhanova str., Vladivostok, 690950, Russian Federation; State Polytechnical University, 29, Polytecnicheskaya str., St.-Petersburg, 195251, Russian Federation","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. © 2014 Elsevier B.V. All rights reserved.","author_keywords":"Antiviral peptides; Influenza A; Influenza A polymerase; PB1","correspondence_address1":"Egorov, V.V.; Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., Russian Federation","publisher":"Elsevier B.V.","issn":"01663542","coden":"ARSRD","pubmed_id":"25446335","language":"English","abbrev_source_title":"Antiviral Res.","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Matusevich20154,\r\nauthor={Matusevich, O.V. and Egorov, V.V. and Gluzdikov, I.A. and Titov, M.I. and Zarubaev, V.V. and Shtro, A.A. and Slita, A.V. and Dukov, M.I. and Shurygina, A.-P.S. and Smirnova, T.D. and Kudryavtsev, I.V. and Vasin, A.V. and Kiselev, O.I.},\r\ntitle={Synthesis and antiviral activity of PB1 component of the influenza A RNA polymerase peptide fragments},\r\njournal={Antiviral Research},\r\nyear={2015},\r\nvolume={113},\r\npages={4-10},\r\ndoi={10.1016/j.antiviral.2014.10.015},\r\nnote={cited By 6},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84911884647&doi=10.1016%2fj.antiviral.2014.10.015&partnerID=40&md5=ee11406f9aea9680cc6c4c4cec4df9af},\r\naffiliation={Saint Petersburg State University, Faculty of Chemistry, 26, Universitetskii pr., Petrodvorets, St.-Petersburg, 198504, Russian Federation; Research Institute of Influenza, Molecular Virology Department, 15/17, Prof. Popova str., St.-Petersburg, 197376, Russian Federation; Inst. of Experimental Medicine of the North-West Branch of the Russian Academy of Medical Sciences, 12, Akad. Pavlova str., St.-Petersburg, 197376, Russian Federation; Petersburg Nuclear Physics Institute, NRC KI, Orlova roscha, Gatchina, 188300, Russian Federation; Far East Federal University, 8, Suhanova str., Vladivostok, 690950, Russian Federation; State Polytechnical University, 29, Polytecnicheskaya str., St.-Petersburg, 195251, Russian Federation},\r\nabstract={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. © 2014 Elsevier B.V. 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