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Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide
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Rekke forfattare: 112017 (engelsk)Inngår i: eLIFE, E-ISSN 2050-084X, Vol. 6, artikkel-id e26067Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

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2017. Vol. 6, artikkel-id e26067
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-147160DOI: 10.7554/eLife.26067ISI: 000408198100001OAI: oai:DiVA.org:su-147160DiVA, id: diva2:1143813
Tilgjengelig fra: 2017-09-22 Laget: 2017-09-22 Sist oppdatert: 2022-03-23bibliografisk kontrollert

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