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In vitro quantification of the effects of IP6 and other small polyanions on immature hiv-1 particle assembly and core stability

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F20%3A43920757" target="_blank" >RIV/60461373:22330/20:43920757 - isvavai.cz</a>

  • Result on the web

    <a href="https://jvi.asm.org/content/94/20/e00991-20" target="_blank" >https://jvi.asm.org/content/94/20/e00991-20</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1128/JVI.00991-20" target="_blank" >10.1128/JVI.00991-20</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    In vitro quantification of the effects of IP6 and other small polyanions on immature hiv-1 particle assembly and core stability

  • Original language description

    Proper assembly and disassembly of both immature and mature HIV-1 hexameric lattices are critical for successful viral replication. These processes are facilitated by several host-cell factors, one of which is myo-inositol hexaphosphate (IP6). IP6 participates in the proper assembly of Gag into immature hexameric lattices and is incorporated into HIV-1 particles. Following maturation, IP6 is also likely to participate in stabilizing capsid protein-mediated mature hexameric lattices. Although a structural-functional analysis of the importance of IP6 in the HIV-1 life cycle has been reported, the effect of IP6 has not yet been quantified. Using two in vitro methods, we quantified the effect of IP6 on the assembly of immature-like HIV-1 particles, as well as its stabilizing effect during disassembly of mature-like particles connected with uncoating. We analyzed a broad range of molar ratios of protein hexamers to IP6 molecules during assembly and disassembly. The specificity of the IP6-facilitated effect on HIV-1 particle assembly and stability was verified by K290A, K359A, and R18A mutants. In addition to IP6, we also tested other polyanions as potential assembly cofactors or stabilizers of viral particles. © 2020 American Society for Microbiology.

  • 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

    <a href="/en/project/GA20-19906S" target="_blank" >GA20-19906S: Modulation of capsid protein hexameric lattice stability: a promising target for HIV-1 inhibition</a><br>

  • 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

    Journal of Virology

  • ISSN

    0022-538X

  • e-ISSN

  • Volume of the periodical

    94

  • Issue of the periodical within the volume

    20

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

  • UT code for WoS article

    000579827700010

  • EID of the result in the Scopus database

    2-s2.0-85092332116