Abstract:
:The α-helical (AH) domain of the hepatitis C virus nonstructural protein NS5A, anchored at the cytoplasmic leaflet of the endoplasmic reticulum, plays a role in viral replication. However, the peptides derived from this domain also exhibit remarkably broad-spectrum virocidal activity, raising questions about their modes of membrane association. Here, using giant lipid vesicles, we show that the AH peptide discriminates between membrane compositions. In cholesterol-containing membranes, peptide binding induces microdomain formation. By contrast, cholesterol-depleted membranes undergo global softening at elevated peptide concentrations. Furthermore, in mixed populations, the presence of ∼100 nm vesicles of viral dimensions suppresses these peptide-induced perturbations in giant unilamellar vesicles, suggesting size-dependent membrane association. These synergistic composition- and size-dependent interactions explain, in part, how the AH domain might on the one hand segregate molecules needed for viral assembly and on the other hand furnish peptides that exhibit broad-spectrum virocidal activity.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Hanson JM,Gettel DL,Tabaei SR,Jackman J,Kim MC,Sasaki DY,Groves JT,Liedberg B,Cho NJ,Parikh ANdoi
10.1016/j.bpj.2015.11.032subject
Has Abstractpub_date
2016-01-05 00:00:00pages
176-87issue
1eissn
0006-3495issn
1542-0086pii
S0006-3495(15)01215-1journal_volume
110pub_type
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