@article{PAR00000160,
  title = {{I}dentification and functional analysis of {VP}3, the guanylyltransferase of {B}anna virus (genus {S}eadornavirus, family {R}eoviridae)},
  author = {{J}aafar, {F}.{M}. and {A}ttoui, {H}. and {M}ertens, {P}.{P}.{C}. and de {M}icco, {P}. and {L}amballerie, {X}avier de},
  editor = {},
  language = {{ENG}},
  abstract = {{B}anna virus ({BAV}) particles contain seven structural proteins: {VP}4 and {VP}9 form an outer-capsid layer, whilst the virus core contains three major proteins ({VP}2, {VP}8 and {VP}10) and two minor proteins ({VP}1 and {VP}3). {S}equence analysis showed that {VP}3 contains motifs [{K}x({I}/{V}/{L}){S}] and ({H}x,{H}) that have previously been identified in the guanylyltransferases of other reoviruses. {I}ncubation of purified {BAV}-{C}h core particles with [alpha-{P}-32]{GTP} resulted in exclusive covalent labelling of {VP}3, demonstrating autoguanylation activity (which is considered indicative of guanylyltransferase activity). {R}ecombinant {VP}3 prepared in a cell-free expression system was also guanylated under similar reaction conditions, and products were synthesized (in the presence of non-radiolabelled {GDP}) that co-migrated with {GMP}, {GDP} and {G}ppp{G} during {TLC}. {T}his reaction, which required magnesium ions for optimum activity, demonstrates that {VP}3 possesses nucleoside triphosphatase ({GTP}ase) activity and is the {BAV} guanylyltransferase ({RNA} 'capping' enzyme).},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {G}eneral {V}irology},
  volume = {86 {P}art 4},
  numero = {},
  pages = {1141--1146},
  ISSN = {0022-1317},
  year = {2005},
  DOI = {10.1099/vir.0.80579-0},
  URL = {https://www.documentation.ird.fr/hor/{PAR}00000160},
}