@article{fdi:010042956,
  title = {{A}ntigenic conservation and immunogenicity of the {HIV} coreceptor binding site},
  author = {{D}ecker, {J}.{M}. and {B}ibollet {R}uche, {F}. and {W}ei, {X}.{P}. and {W}ang, {S}.{Y}. and {L}evy, {D}.{N}. and {W}ang, {W}.{Q}. and {D}elaporte, {E}ric and {P}eeters, {M}artine and {D}erdeyn, {C}.{A}. and {A}llen, {S}. and {H}unter, {E}. and {S}aag, {M}.{S}. and {H}oxie, {J}.{A}. and {H}ahn, {B}.{H}. and {K}wong, {P}.{D}. and {R}obinson, {J}.{E}. and {S}haw, {G}.{M}.},
  editor = {},
  language = {{ENG}},
  abstract = {{I}mmunogenic, broadly reactive epitopes of the {HIV}-1 envelope glycoprotein could serve as important targets of the adaptive humoral immune response in natural infection and, potentially, as components of an acquired immune deficiency syndrome vaccine. {H}owever, variability in exposed epitopes and a combination of highly effective envelope-cloaking strategies have made the identification of such epitopes problematic. {H}ere, we show that the chemokine coreceptor binding site of {HIV}-1 from clade {A}, {B}, {C}, {D}, {F}, {G}, and {H} and circulating recombinant form ({CRF})01, {CRF}02, and {CRF}11, elicits high titers of {CD}4-induced ({CD}4i) antibody during natural human infection and that these antibodies bind and neutralize viruses as divergent as {HIV}-2 in the presence of soluble {CD}4 (s{CD}4). 178 out of 189 (94%) {HIV}-1-infected patients had {CD}4i antibodies that neutralized s{CD}4-pretreated {HIV}-2 in titers (50% inhibitory concentration) as high as 1:143,000. {CD}4i monoclonal antibodies elicited by {HIV}-1 infection also neutralized {HIV}-2 pretreated with s{CD}4, and polyclonal antibodies from {HIV}-1-infected humans competed specifically with such monoclonal antibodies for binding. {I}n vivo, variants of {HIV}-1 with spontaneously exposed coreceptor binding surfaces were detected in human plasma; these viruses were neutralized directly by {CD}4i antibodies. {D}espite remarkable evolutionary diversity among primate lentiviruses, functional constraints on receptor binding create opportunities for broad humoral immune recognition, which in turn serves to constrain the viral quasispecies.},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {E}xperimental {M}edicine},
  volume = {201},
  numero = {9},
  pages = {1407--1419},
  ISSN = {0022-1007},
  year = {2005},
  DOI = {10.1084/jem.20042510},
  URL = {https://www.documentation.ird.fr/hor/fdi:010042956},
}