All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

A simple, high-throughput stabilization assay to test HIV-1 uncoating inhibitors

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00517403" target="_blank" >RIV/61388963:_____/19:00517403 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22330/19:43919093 RIV/60461373:22810/19:43919093

  • Result on the web

    <a href="https://www.nature.com/articles/s41598-019-53483-w" target="_blank" >https://www.nature.com/articles/s41598-019-53483-w</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41598-019-53483-w" target="_blank" >10.1038/s41598-019-53483-w</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A simple, high-throughput stabilization assay to test HIV-1 uncoating inhibitors

  • Original language description

    Shortly after entering the cell, HIV-1 copies its genomic RNA into double-stranded DNA in a process known as reverse transcription. This process starts inside a core consisting of an enclosed lattice of capsid proteins that protect the viral RNA from cytosolic sensors and degradation pathways. To accomplish reverse transcription and integrate cDNA into the host cell genome, the capsid shell needs to be disassembled, or uncoated. Premature or delayed uncoating attenuates reverse transcription and blocks HIV-1 infectivity. Small molecules that bind to the capsid lattice of the HIV-1 core and either destabilize or stabilize its structure could thus function as effective HIV-1 inhibitors. To screen for such compounds, we modified our recently developed FAITH assay to allow direct assessment of the stability of in vitro preassembled HIV-1 capsid-nucleocapsid (CANC) tubular particles. This new assay is a high-throughput fluorescence method based on measuring the amount of nucleic acid released from CANC complexes under disassembly conditions. The amount of disassembled CANC particles and released nucleic acid is proportional to the fluorescence signal, from which the relative percentage of CANC stability can be calculated. We consider our assay a potentially powerful tool for in vitro screening for compounds that alter HIV disassembly.

  • 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

    <a href="/en/project/GA17-25602S" target="_blank" >GA17-25602S: Study of the role of capsid protein in early phase of HIV-1 replication cycle using the newly identified compounds stabilizing capsid complexes</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    Scientific Reports

  • ISSN

    2045-2322

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    Nov 19

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    12

  • Pages from-to

    17076

  • UT code for WoS article

    000497701800033

  • EID of the result in the Scopus database

    2-s2.0-85075205104