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Structural characterization of the interaction between the C-terminal domain of the influenza polymerase PA subunit and an optimized small peptide inhibitor
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SYSNO ASEP 0536615 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural characterization of the interaction between the C-terminal domain of the influenza polymerase PA subunit and an optimized small peptide inhibitor Author(s) Hejdánek, Jakub (UOCHB-X)
Radilová, Kateřina (UOCHB-X) ORCID
Pachl, Petr (UOCHB-X) RID, ORCID
Hodek, Jan (UOCHB-X) RID, ORCID
Machara, Aleš (UOCHB-X) ORCID
Weber, Jan (UOCHB-X) RID, ORCID
Řezáčová, Pavlína (UOCHB-X) RID, ORCID
Konvalinka, Jan (UOCHB-X) RID, ORCID
Kožíšek, Milan (UOCHB-X) RID, ORCIDArticle number 104971 Source Title Antiviral Research. - : Elsevier - ISSN 0166-3542
Roč. 185, Jan (2021)Number of pages 7 s. Language eng - English Country NL - Netherlands Keywords antiviral peptides ; influenza a polymerase ; protein-protein interaction ; AlphaScreen OECD category Biochemistry and molecular biology R&D Projects EF16_019/0000729 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2018133 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UOCHB-X - RVO:61388963 UT WOS 000604747500003 EID SCOPUS 85096015372 DOI 10.1016/j.antiviral.2020.104971 Annotation Influenza viruses can cause severe respiratory infections in humans, leading to nearly half a million deaths worldwide each year. Improved antiviral drugs are needed to address the threat of development of novel pandemic strains. Current therapeutic interventions target three key proteins in the viral life cycle: neuraminidase, the M2 channel and RNA-dependent-RNA polymerase. Protein-protein interactions between influenza polymerase subunits are potential new targets for drug development. Using a newly developed assay based on AlphaScreen technology, we screened a peptide panel for protein-protein interaction inhibitors to identify a minimal PB1 subunit-derived peptide that retains high inhibition potential and can be further modified. Here, we present an X-ray structure of the resulting decapeptide bound to the C-terminal domain of PA polymerase subunit from pandemic isolate A/California/07/2009 H1N1 at 1.6 Å resolution and discuss its implications for the design of specific, potent influenza polymerase inhibitors. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2022 Electronic address https://doi.org/10.1016/j.antiviral.2020.104971
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