Abstract:
:Positive strand RNA viruses replicate in specialized niches called membranous web within the cytoplasm of host cells. These virus replication organelles sequester viral proteins, RNA, and a variety of host factors within a fluid, amorphous matrix of clusters of endoplasmic reticulum (ER) derived vesicles. They are thought to form by the actions of a nonstructural viral protein NS4B, which remodels the ER and produces dense lipid-protein condensates. Here, we used in vitro reconstitution to identify the minimal components and elucidate physical mechanisms driving the web formation. We found that the N-terminal amphipathic domain of NS4B (peptide 4BAH2) and phospholipid vesicles (∼100-200 nm in diameter) were sufficient to produce a gel-like, viscoelastic condensate. This condensate coexists with the surrounding aqueous phase and affords rapid exchange of molecules. Together, it recapitulates the essential properties of the virus-induced membranous web. Our data support a novel phase separation mechanism in which phospholipid vesicles provide a supramolecular template spatially organizing multiple self-associating peptides thereby generating programmable multivalency de novo and inducing macroscopic phase separation.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Ho JCS,Steininger C,Hiew SH,Kim MC,Reimhult E,Miserez A,Cho N,Parikh AN,Liedberg Bdoi
10.1021/acs.biomac.9b00081subject
Has Abstractpub_date
2019-04-08 00:00:00pages
1709-1718issue
4eissn
1525-7797issn
1526-4602journal_volume
20pub_type
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