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Oligomerization and assembly of the matrix protein of Borna disease virus
Author(s) -
Kraus Ina,
Bogner Elke,
Lilie Hauke,
Eickmann Markus,
Garten Wolfgang
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.002
Subject(s) - recombinant dna , ultracentrifuge , chemistry , virus , capsid , viral matrix protein , size exclusion chromatography , escherichia coli , covalent bond , virus like particle , electron microscope , viral envelope , molecular mass , biophysics , virology , crystallography , biology , biochemistry , physics , gene , enzyme , organic chemistry , optics
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 Å 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.