Complement Activation Selectively Potentiates the Pathogenicity of the IgG2b and IgG3 Isotypes of a High Affinity Anti-Erythrocyte Autoantibody

@article{Silveira2002ComplementAS,
  title={Complement Activation Selectively Potentiates the Pathogenicity of the IgG2b and IgG3 Isotypes of a High Affinity Anti-Erythrocyte Autoantibody},
  author={Samareh Azeredo da Silveira and Shuichi Kikuchi and Liliane Fossati-Jimack and Thomas Moll and Takashi K. Saito and J Sjef Verbeek and Marina Botto and Mark J. Walport and Michael C Carroll and Shozo Izui},
  journal={The Journal of Experimental Medicine},
  year={2002},
  volume={195},
  pages={665 - 672}
}
By generating four IgG isotype-switch variants of the high affinity 34-3C anti-erythrocyte autoantibody, and comparing them to the IgG variants of the low affinity 4C8 anti-erythrocyte autoantibody that we have previously studied, we evaluated in this study how high affinity binding to erythrocytes influences the pathogenicity of each IgG isotype in relation to the respective contributions of Fcgamma receptor (FcgammaR) and complement. The 34-3C autoantibody opsonizing extensively circulating… CONTINUE READING
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Markedly different pathogenicity of four IgG isotype-switch variants of an anti-erythrocyte autoantibody is based on their respective capacity to interact in vivo with the low-affinity Fc RIII

  • L. Fossati-Jimack, A. Ioan-Facsinay, +7 authors R. E. Schmidt
  • J. Exp. Med
  • 2000
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