Mutation of the Highly Conserved Ser-40 of the HIV-1 p6 Gag Protein to Phe Causes the Formation of a Hydrophobic Patch, Enhances Membrane Association, and Polyubiquitination of Gag

Mutation of the Highly Conserved Ser-40 of the HIV-1 p6 Gag Protein to Phe Causes the Formation of a Hydrophobic Patch, Enhances Membrane Association, and Polyubiquitination of Gag

The HIV-1 p6 Gag protein contains two late assembly (l-) domains that recruit proteins of the endosomal sorting complex required for transport (ESCRT) pathway to mediate membrane fission between the nascent virion and the cell membrane. It was recently demonstrated that mutation of the highly conser...

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Bibliographic Details
Main Authors: Friedrich Hahn, Christian Setz, Melanie Friedrich, Pia Rauch, Sara Marie Solbak, Nils Åge Frøystein, Petra Henklein, Jörg Votteler, Torgils Fossen, Ulrich Schubert
Format: Article
Language:English
Published: MDPI AG 2014-10-01
Series:Viruses
Subjects:
HIV-1
Gag p6
ubiquitination
virus budding
membrane association
Online Access:http://www.mdpi.com/1999-4915/6/10/3738

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