@article{PAR00006107,
  title = {{G}enomics and structure/function studies of {R}habdoviridae proteins involved in replication and transcription},
  author = {{A}ssenberg, {R}. and {D}elmas, {O}. and {M}orin, {B}. and {G}raham, {S}. {C}. and de {L}amballerie, {X}avier and {L}aubert, {C}. and {C}outard, {B}. and {G}rimes, {J}. {M}. and {N}eyts, {J}. and {O}wens, {R}. {J}. and {B}randt, {B}. {W}. and {G}orbalenya, {A}. and {T}ucker, {P}. and {S}tuart, {D}. {I}. and {C}anard, {B}. and {B}ourhy, {H}.},
  editor = {},
  language = {{ENG}},
  abstract = {{S}ome mammalian rhabdoviruses may infect humans, and also infect invertebrates, dogs, and bats, which may act as vectors transmitting viruses among different host species. {T}he {VIZIER} programme, an {EU}-funded {FP}6 program, has characterized viruses that belong to the {V}esiculovirus, {E}phemerovirus and {L}yssavirus genera of the {R}habdoviridae family to perform ground-breaking research on the identification of potential new drug targets against these {RNA} viruses through comprehensive structural characterization of the replicative machinery. {T}he contribution of {VIZIER} programme was of several orders. {F}irst, it contributed substantially to research aimed at understanding the origin, evolution and diversity of rhabdoviruses. {T}his diversity was then used to obtain further structural information on the proteins involved in replication. {T}wo strategies were used to produce recombinant proteins by expression of both full length or domain constructs in either {E}. coil or insect cells, using the baculovirus system. {I}n both cases, parallel cloning and expression screening at small-scale of multiple constructs based on different viruses including the addition of fusion tags, was key to the rapid generation of expression data. {A}s a result, some progress has been made in the {VIZIER} programme towards dissecting the multi-functional {L} protein into components suitable for structural and functional studies. {H}owever, the phosphoprotein polymerase co-factor and the structural matrix protein, which play a number of roles during viral replication and drives viral assembly, have both proved much more amenable to structural biology. {A}pplying the multi-construct/multi-virus approach central to protein production processes in {VIZIER} has yielded new structural information which may ultimately be exploitable in the derivation of novel ways of intervening in viral replication.},
  keywords = {{R}habdovirus ; {V}iral replication ; {V}iral evolution ; {RNA} viruses ; {M}ononegavirales ; {A}ntiviral therapy},
  booktitle = {},
  journal = {{A}ntiviral {R}esearch},
  volume = {87},
  numero = {2},
  pages = {149--161},
  ISSN = {0166-3542},
  year = {2010},
  DOI = {10.1016/j.antiviral.2010.02.322},
  URL = {https://www.documentation.ird.fr/hor/{PAR}00006107},
}