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PF74 and its novel derivatives stabilize hexameric lattice of HIV-1 mature-like particles

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F20%3A43920760" target="_blank" >RIV/60461373:22330/20:43920760 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22810/20:43920760

  • Result on the web

    <a href="http://file:///C:/Users/kasparkh/AppData/Local/Temp/molecules-25-01895.pdf" target="_blank" >http://file:///C:/Users/kasparkh/AppData/Local/Temp/molecules-25-01895.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/molecules25081895" target="_blank" >10.3390/molecules25081895</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    PF74 and its novel derivatives stabilize hexameric lattice of HIV-1 mature-like particles

  • Original language description

    A major structural retroviral protein, capsid protein (CA), is able to oligomerize into two different hexameric lattices, which makes this protein a key component for both the early and late stages of HIV-1 replication. During the late stage, the CA protein, as part of the Gag polyprotein precursor, facilitates protein–protein interactions that lead to the assembly of immature particles. Following protease activation and Gag polyprotein processing, CA also drives the assembly of the mature viral core. In the early stage of infection, the role of the CA protein is distinct. It controls the disassembly of the mature CA hexameric lattice i.e., uncoating, which is critical for the reverse transcription of the single-stranded RNA genome into double stranded DNA. These properties make CA a very attractive target for small molecule functioning as inhibitors of HIV-1 particle assembly and/or disassembly. Of these, inhibitors containing the PF74 scaffold have been extensively studied. In this study, we reported a series of modifications of the PF74 molecule and its characterization through a combination of biochemical and structural approaches. Our data supported the hypothesis that PF74 stabilizes the mature HIV-1 CA hexameric lattice. We identified derivatives with a higher in vitro stabilization activity in comparison to the original PF74 molecule. © 2020 by the authors.

  • 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

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecules

  • ISSN

    1420-3049

  • e-ISSN

  • Volume of the periodical

    25

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    22

  • Pages from-to

  • UT code for WoS article

    000534617300073

  • EID of the result in the Scopus database

    2-s2.0-85083579094