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Updated: Jun 18, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
Published on: July 28, 2022
Chapter 4 - Reconstitution of membrane budding with unilamellar vesicles
Anna V Shnyrova1, Joshua Zimmerberg
1Laboratory of Cellular and Molecular Biology, Program in Physical Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, Maryland, USA.
None:
Enveloped virus particles select their lipid-protein components and egress by budding from the host cell membranes. The matrix protein of many enveloped viruses has been proposed as a crucial element for viral budding; however, molecular mechanisms behind membrane remodeling by the matrix protein are yet to be unraveled. Here, we describe a set of in vitro functional reconstitution assays that allow quantitative evaluation of both, membrane binding and creation of membrane curvature by the matrix protein isolated from Newcastle Disease Virus. Individual budding events orchestrated by the matrix protein can be resolved in real time. The assays may be applied for direct reconstitution of the on-membrane action of cellular proteins involved in membrane curvature induction upon binding in vivo.
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