%0 Journal Article
%9 ACL : Articles dans des revues avec comité de lecture répertoriées par l'AERES
%A Lecorre, F.
%A Lai-Kee-Him, J.
%A Blanc, S.
%A Zeddam, Jean-Louis
%A Trapani, S.
%A Bron, P.
%T The cryo-electron microscopy structure of Broad Bean Stain Virus suggests a common capsid assembly mechanism among comoviruses
%D 2019
%L fdi:010075598
%G ENG
%J Virology
%@ 0042-6822
%K Cryo-EM ; Three-dimensional structure ; Single-particle analysis ; BBSV ; Comovirus ; Virus coat protein ; Single-stranded RNA genome
%M ISI:000464770400010
%P 75-84
%R 10.1016/j.virol.2019.02.009
%U https://www.documentation.ird.fr/hor/fdi:010075598
%> https://www.documentation.ird.fr/intranet/publi/2019/05/010075598.pdf
%V 530
%W Horizon (IRD)
%X The Broad bean stain virus (BBSV) is a member of the genus Comovirus infecting Fabaceae. The virus is transmitted through seed and by plant weevils causing severe and widespread disease worldwide. BBSV has a bipartite, positive-sense, single-stranded RNA genome encapsidated in icosahedral particles. We present here the cryo-electron microscopy reconstruction of the BBSV and an atomic model of the capsid proteins refined at 3.22 angstrom resolution. We identified residues involved in RNA/capsid interactions revealing a unique RNA genome organization. Inspection of the small coat protein C-terminal domain highlights a maturation cleavage between Leu567 and Leu568 and interactions of the C-terminal stretch with neighbouring small coat proteins within the capsid pentameric turrets. These interactions previously proposed to play a key role in the assembly of the Cowpea mosaic virus suggest a common capsid assembly mechanism throughout all comovirus species.
%$ 076 ; 020