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Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F75010330%3A_____%2F17%3A00011797" target="_blank" >RIV/75010330:_____/17:00011797 - isvavai.cz</a>

  • Result on the web

    <a href="https://elifesciences.org/articles/26067" target="_blank" >https://elifesciences.org/articles/26067</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.7554/eLife.26067" target="_blank" >10.7554/eLife.26067</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide

  • Original language description

    Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the endoplasmic reticulum (ER) by its signal peptide during synthesis. Proper gp160 folding in the ER requires core glycosylation, disulfide-bond formation and proline isomerization. Signal-peptide cleavage occurs only late after gp160 chain termination and is dependent on folding of the soluble subunit gp120 to a near-native conformation. We here detail the mechanism by which co-translational signal-peptide cleavage is prevented. Conserved residues from the signal peptide and residues downstream of the canonical cleavage site form an extended alpha-helix in the ER membrane, which covers the cleavage site, thus preventing cleavage. A point mutation in the signal peptide breaks the alpha helix allowing co-translational cleavage. We demonstrate that postponed cleavage of gp160 enhances functional folding of the molecule. The change to early cleavage results in decreased viral fitness compared to wild-type HIV.

  • 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

    30303 - Infectious Diseases

Result continuities

  • Project

  • Continuities

    N - Vyzkumna aktivita podporovana z neverejnych zdroju

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    eLIFE

  • ISSN

    2050-084X

  • e-ISSN

  • Volume of the periodical

    6

  • Issue of the periodical within the volume

    July

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    25

  • Pages from-to

    nestrankovano

  • UT code for WoS article

    000408198100001

  • EID of the result in the Scopus database