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Stimulated Emission Depletion Nanoscopy Reveals Time-Course of Human Immunodeficiency Virus Proteolytic Maturation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00466278" target="_blank" >RIV/61388963:_____/16:00466278 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/16:10331060

  • Result on the web

    <a href="http://dx.doi.org/10.1021/acsnano.6b03850" target="_blank" >http://dx.doi.org/10.1021/acsnano.6b03850</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acsnano.6b03850" target="_blank" >10.1021/acsnano.6b03850</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Stimulated Emission Depletion Nanoscopy Reveals Time-Course of Human Immunodeficiency Virus Proteolytic Maturation

  • Original language description

    Concomitant with human immunodeficiency virus-type 1 (HIV-1) budding from a host cell, cleavage of the structural Gag polyproteins by the viral protease (PR) triggers complete remodeling of virion architecture. This maturation process is essential for virus infectivity. Electron tomography provided structures of immature and mature HIV-1 with a diameter of 120-140 nm, but information about the sequence and dynamics of structural rearrangements is lacking. Here, we employed super-resolution STED (stimulated emission depletion) fluorescence nanoscopy of HIV-1 carrying labeled Gag to visualize the virion architecture. The incomplete Gag lattice of immature virions was dearly distinguishable from the condensed distribution of mature protein subunits. Synchronized activation of PR-within purified particles by photocleavage of a caged PR inhibitor enabled time-resolved in situ observation of the induction of proteolysis and maturation by super-resolution microscopy. This study shows the rearrangement of subviral structures in a super resolution light microscope over time, outwitting phototoxicity and fluorophore bleaching through synchronization of a biological process by an optical switch.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    ACS Nano

  • ISSN

    1936-0851

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    8215-8222

  • UT code for WoS article

    000384399300012

  • EID of the result in the Scopus database

    2-s2.0-84989201915