Oligomerization and assembly of the matrix protein of Borna disease virus.

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 Lett

journal_title

FEBS letters

authors

Kraus I,Bogner E,Lilie H,Eickmann M,Garten W

doi

10.1016/j.febslet.2005.04.002

keywords:

subject

Has Abstract

pub_date

2005-05-09 00:00:00

pages

2686-92

issue

12

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00456-4

journal_volume

579

pub_type

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