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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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00536615" target="_blank" >RIV/61388963:_____/21:00536615 - isvavai.cz</a>

  • Alternative codes found

    RIV/68378050:_____/21:00544819 RIV/00216208:11110/21:10425868 RIV/00216208:11310/21:10425868

  • Result on the web

    <a href="https://doi.org/10.1016/j.antiviral.2020.104971" target="_blank" >https://doi.org/10.1016/j.antiviral.2020.104971</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.antiviral.2020.104971" target="_blank" >10.1016/j.antiviral.2020.104971</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structural characterization of the interaction between the C-terminal domain of the influenza polymerase PA subunit and an optimized small peptide inhibitor

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Antiviral Research

  • ISSN

    0166-3542

  • e-ISSN

    1872-9096

  • Volume of the periodical

    185

  • Issue of the periodical within the volume

    Jan

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    7

  • Pages from-to

    104971

  • UT code for WoS article

    000604747500003

  • EID of the result in the Scopus database

    2-s2.0-85096015372