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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kraus I,Bogner E,Lilie H,Eickmann M,Garten Wdoi
10.1016/j.febslet.2005.04.002keywords:
subject
Has Abstractpub_date
2005-05-09 00:00:00pages
2686-92issue
12eissn
0014-5793issn
1873-3468pii
S0014-5793(05)00456-4journal_volume
579pub_type
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