Oligomerization and assembly of the matrix protein of Borna disease virus.
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.
Kraus
Ina
I
Institut für Virologie, Marburg, Germany.
Bogner
Elke
E
Lilie
Hauke
H
Eickmann
Markus
M
Garten
Wolfgang
W
D001891:Borna disease virus / Q000737:chemistry* / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003432:Cross-Linking Reagents / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D011489:Protein Denaturation; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014461:Ultracentrifugation; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D019065:Virus Assembly / Q000502:physiology*
D003432:Cross-Linking Reagents; D014763:Viral Matrix Proteins