@article{fdi:010075598,
  title = {{T}he cryo-electron microscopy structure of {B}road {B}ean {S}tain {V}irus suggests a common capsid assembly mechanism among comoviruses},
  author = {{L}ecorre, {F}. and {L}ai-{K}ee-{H}im, {J}. and {B}lanc, {S}. and {Z}eddam, {J}ean-{L}ouis and {T}rapani, {S}. and {B}ron, {P}.},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he {B}road bean stain virus ({BBSV}) is a member of the genus {C}omovirus infecting {F}abaceae. {T}he 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. {W}e present here the cryo-electron microscopy reconstruction of the {BBSV} and an atomic model of the capsid proteins refined at 3.22 angstrom resolution. {W}e identified residues involved in {RNA}/capsid interactions revealing a unique {RNA} genome organization. {I}nspection of the small coat protein {C}-terminal domain highlights a maturation cleavage between {L}eu567 and {L}eu568 and interactions of the {C}-terminal stretch with neighbouring small coat proteins within the capsid pentameric turrets. {T}hese interactions previously proposed to play a key role in the assembly of the {C}owpea mosaic virus suggest a common capsid assembly mechanism throughout all comovirus species.},
  keywords = {{C}ryo-{EM} ; {T}hree-dimensional structure ; {S}ingle-particle analysis ; {BBSV} ; {C}omovirus ; {V}irus coat protein ; {S}ingle-stranded {RNA} genome},
  booktitle = {},
  journal = {{V}irology},
  volume = {530},
  numero = {},
  pages = {75--84},
  ISSN = {0042-6822},
  year = {2019},
  DOI = {10.1016/j.virol.2019.02.009},
  URL = {https://www.documentation.ird.fr/hor/fdi:010075598},
}