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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30303 - Infectious Diseases
Result continuities
Project
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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
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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
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