@article{fdi:010071980,
  title = {{F}irst experimental assessment of protein intrinsic disorder involvement in an {RNA} virus natural adaptive process},
  author = {{C}haron, {J}. and {B}arra, {A}. and {W}alter, {J}. and {M}illot, {P}. and {H}{\'e}brard, {E}ug{\'e}nie and {M}oury, {B}. and {M}ichon, {T}.},
  editor = {},
  language = {{ENG}},
  abstract = {{I}ntrinsic disorder ({ID}) in proteins is defined as a lack of stable structure in physiological conditions. {I}ntrinsically disordered regions ({IDR}s) are highly abundant in some {RNA} virus proteomes. {L}ow topological constraints exerted on {IDR}s are expected to buffer the effect of numerous deleterious mutations and could be related to the remarkable adaptive potential of {RNA} viruses to overcome resistance of their host. {T}o experimentally test this hypothesis in a natural pathosystem, a set of four variants of {P}otato virus {Y} ({PVY}; {P}otyvirus genus) containing various {ID} degrees in the {V}iral genome-linked ({VP}g) protein, a key determinant of potyvirus adaptation, was designed. {T}o estimate the {ID} contribution to the {VP}g-based {PVY} adaptation, the adaptive ability of the four {PVY} variants was monitored in the pepper host ({C}apsicum annuum) carrying a recessive resistance gene. {I}ntriguingly, the two mutants with the highest {ID} content displayed a significantly higher ability to restore infection in the resistant host, whereas the less intrinsically disordered mutant was unable to restore infection. {T}he role of {ID} on virus adaptation may be due either to a larger exploration of evolutionary pathways or the minimization of fitness penalty caused by resistance-breaking mutations. {T}his pioneering study strongly suggests the positive impact of {ID} in an {RNA} virus adaptive capacity.},
  keywords = {protein intrinsic disorder ; potyvirus ; {RNA} virus adaptation ; resistance ; breakdown ; viral protein genome-linked ; eukaryotic translation ; initiation factor 4{E}},
  booktitle = {},
  journal = {{M}olecular {B}iology and {E}volution},
  volume = {35},
  numero = {1},
  pages = {38--49},
  ISSN = {0737-4038},
  year = {2018},
  DOI = {10.1093/molbev/msx249},
  URL = {https://www.documentation.ird.fr/hor/fdi:010071980},
}