Please use this identifier to cite or link to this item:
Title: Minimal reconstitution of membranous web induced by a vesicle–peptide sol–gel transition
Authors: Ho, James Chin Shing
Steininger, Christoph
Hiew, Shu Hui
Kim, Min Chul
Reimhult, Erik
Miserez, Ali
Cho, Nam-Joon
Parikh, Atul N.
Liedberg, Bo
Keywords: Engineering::Chemical engineering
Issue Date: 2019
Source: Ho, J. C. S., Steininger, C., Hiew, S. H., Kim, M. C., Reimhult, E., Miserez, A., ... Liedberg, B. (2019). Minimal reconstitution of membranous web induced by a vesicle–peptide sol–gel transition. Biomacromolecules, 20(4), 1709-1718. doi:10.1021/acs.biomac.9b00081
Journal: Biomacromolecules
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.
ISSN: 1525-7797
DOI: 10.1021/acs.biomac.9b00081
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biomacromolecules, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

Citations 50

Updated on Mar 10, 2021

Page view(s)

Updated on Jan 19, 2022


Updated on Jan 19, 2022

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.