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A 2.8-Angstrom-Resolution Cryo-Electron Microscopy Structure of Human Parechovirus 3 in Complex with Fab from a Neutralizing Antibody

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90043%2F19%3A00136203" target="_blank" >RIV/00216224:90043/19:00136203 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.pnas.org/doi/epdf/10.1073/pnas.1904732116" target="_blank" >https://www.pnas.org/doi/epdf/10.1073/pnas.1904732116</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1128/JVI.01597-18" target="_blank" >10.1128/JVI.01597-18</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A 2.8-Angstrom-Resolution Cryo-Electron Microscopy Structure of Human Parechovirus 3 in Complex with Fab from a Neutralizing Antibody

  • Original language description

    Human parechovirus 3 (HPeV3) infection is associated with sepsis characterized by significant immune activation and subsequent tissue damage in neonates. Strategies to limit infection have been unsuccessful due to inadequate molecular diagnostic tools for early detection and the lack of a vaccine or specific antiviral therapy. Toward the latter, we present a 2.8-angstrom-resolution structure of HPeV3 in complex with fragments from a neutralizing human monoclonal antibody, AT12-015, using cryo-electron microscopy (cryo-EM) and image reconstruction. Modeling revealed that the epitope extends across neighboring asymmetric units with contributions from capsid proteins VP0, VP1, and VP3. Antibody decoration was found to block binding of HPeV3 to cultured cells. Additionally, at high resolution, it was possible to model a stretch of RNA inside the virion and, from this, identify the key features that drive and stabilize protein-RNA association during assembly.

  • 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

    10607 - Virology

Result continuities

  • Project

  • Continuities

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Virology

  • ISSN

    0022-538X

  • e-ISSN

  • Volume of the periodical

    93

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

    1-12

  • UT code for WoS article

    000457744600013

  • EID of the result in the Scopus database

    2-s2.0-85061740566