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Capsid Structure of Leishmania RNA Virus 1

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F21%3AA22028M2" target="_blank" >RIV/61988987:17310/21:A22028M2 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14740/21:00121505

  • Result on the web

    <a href="https://jvi.asm.org/content/jvi/95/3/e01957-20.full.pdf" target="_blank" >https://jvi.asm.org/content/jvi/95/3/e01957-20.full.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1128/JVI.01957-20" target="_blank" >10.1128/JVI.01957-20</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Capsid Structure of Leishmania RNA Virus 1

  • Original language description

    Leishmania parasites cause a variety of symptoms, including mucocutaneous leishmaniasis, which results in the destruction of the mucous membranes of the nose, mouth, and throat. The species of Leishmania carrying Leishmania RNA virus 1 (LRV1), from the family Totiviridae, are more likely to cause severe disease and are less sensitive to treatment than those that do not contain the virus. Although the importance of LRV1 for the severity of leishmaniasis was discovered a long time ago, the structure of the virus remained unknown. Here, we present a cryo-electron microscopy reconstruction of the virus-like particle of LRV1 determined to a resolution of 3.65 angstrom. The capsid has icosahedral symmetry and is formed by 120 copies of a capsid protein assembled in asymmetric dimers. RNA genomes of viruses from the family Totiviridae are synthetized, but not capped at the 5' end, by virus RNA polymerases. To protect viral RNAs from degradation, capsid proteins of the L-A totivirus cleave the 5' caps of host mRNAs, creating decoys to overload the cellular RNA quality control system. Capsid proteins of LRV1 form positively charged clefts, which may be the cleavage sites for the 5' cap of Leishmania mRNAs. The putative RNA binding site of LRV1 is distinct from that of the related L-A virus. The structure of the LRV1 capsid enables the rational design of compounds targeting the putative decapping site. Such inhibitors may be developed into a treatment for mucocutaneous leishmaniasis caused by LRV1-positive species of Leishmania.

  • 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

    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

    J VIROL

  • ISSN

    0022-538X

  • e-ISSN

    1098-5514

  • Volume of the periodical

    95

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

    e01957-20

  • UT code for WoS article

    000609185100014

  • EID of the result in the Scopus database