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Updated: Aug 18, 2026

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
Published on: March 1, 2012
Oligomerization and assembly of the matrix protein of Borna disease virus
Ina Kraus1, Elke Bogner, Hauke Lilie
1Institut für Virologie, Marburg, Germany.
Abstract:
The matrix protein M of Borna disease virus (BDV) is a constituent of the viral envelope covering the inner leaflet of the lipid bilayer. BDV-M was expressed as recombinant protein in Escherichia coli, purified to homogeneity and structurally analyzed. Recombinant M (i) forms non-covalently bound multimers with a Stoke's radius of 35 Angstroms estimated by size exclusion chromatography, (ii) consists of tetramers detected by analytical ultracentrifugation, and (iii) appears by electron microscopy studies as tetramers with the tendency to assemble into high molecular mass lattice-like complexes. The structural features suggest that BDV-M possesses a dominant driving force for virus particle formation.
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