@article{fdi:010053012,
  title = {{T}he presence of a vpu gene and the lack of nef-mediated downmodulation of {T} cell receptor-{CD}3 are not always linked in primate lentiviruses},
  author = {{S}chmokel, {J}. and {S}auter, {D}. and {S}chindler, {M}. and {L}eendertz, {F}. {H}. and {B}ailes, {E}. and {D}azza, {M}. {C}. and {S}aragosti, {S}. and {B}ibollet {R}uche, {F}. and {P}eeters, {M}artine and {H}ahn, {B}. {H}. and {K}irchhoff, {F}.},
  editor = {},
  language = {{ENG}},
  abstract = {{N}ef is an accessory protein critical for the ability of human and simian immunodeficiency viruses ({HIV} and {SIV}) to replicate efficiently in their respective hosts. {P}revious analyses of members of 15 different primate lentivirus lineages revealed a link between {N}ef function and the presence of a vpu gene. {I}n particular, {N}ef proteins of all vpu-containing viruses had lost their ability to downmodulate the {T} cell ({TCR}-{CD}3) receptor. {H}ere we examined {N}ef proteins from eight additional {SIV} lineages, including {SIV}gor, {SIV}wrc, {SIV}olc, {SIV}gri, {SIV}drl, {SIV}lho, {SIV}den, and {SIV}asc, from western lowland gorillas, western red colobus monkeys, olive colobus monkeys, grivet monkeys, drills, {L}'{H}oest's monkeys, {D}ent's mona monkeys, and red-tailed monkeys, respectively. {W}e found that except for the nef gene of {SIV}drl, all of them were efficiently expressed and modulated {CD}4, major histocompatibility complex class {I} ({MHC}-{I}), {CD}28, {CXCR}4, and {I}i cell surface expression and/or enhanced viral infectivity and replication. {F}urthermore, the {N}ef proteins of {SIV}gri, {SIV}lho, {SIV}wrc, {SIV}olc, and {SIV}gor antagonized tetherin. {A}s expected, the {N}ef protein of {SIV}gor, which carries vpu, failed to downmodulate {CD}3, whereas those of {SIV}wrc, {SIV}gri, {SIV}lho, and {SIV}asc, which lack vpu, were capable of performing this function. {S}urprisingly, however, the {N}ef protein of the vpu-containing {SIV}den strain retained the ability to downmodulate {TCR}-{CD}3, whereas that of {SIV}olc, which does not contain vpu, was unable to perform this function. {A}lthough the {SIV}den {V}pu is about 20 amino acids shorter than other {V}pu proteins, it degrades {CD}4 and antagonizes tetherin. {O}ur data show that there are exceptions to the link between the presence of a vpu gene and nef alleles deficient in {CD}3 modulation, indicating that host properties also affect the selective pressure for {N}ef-mediated disruption of {TCR}-{CD}3 signaling. {O}ur results are also further evidence that tetherin antagonism is a common function of primate lentivirus {N}ef proteins and that the resistance of human tetherin to {N}ef represents a relevant barrier to cross-species transmission of {SIV}s to humans.},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {V}irology},
  volume = {85},
  numero = {2},
  pages = {742--752},
  ISSN = {0022-538{X}},
  year = {2011},
  DOI = {10.1128/jvi.02087-10},
  URL = {https://www.documentation.ird.fr/hor/fdi:010053012},
}