Tolerogenic function of dimeric forms of HLA-g recombinant proteins: A comparative study in Vivo

Benoit Favier, Kiave Yune HoWangYin, Juan Wu, Julien Caumartin, Marina Daouya, Anatolij Horuzsko, Edgardo D. Carosella, Joel Le Maoult

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15 Scopus citations


HLA-G is a natural tolerogenic molecule involved in the best example of tolerance to foreign tissues there is: the maternal-fetal tolerance. The further involvement of HLA-G in the tolerance of allogeneic transplants has also been demonstrated and some of its mechanisms of action have been elucidated. For these reasons, therapeutic HLA-G molecules for tolerance induction in transplantation are actively investigated. In the present study, we studied the tolerogenic functions of three different HLA-G recombinant proteins: HLA-G heavy chain fused to β2-microglobulin (B2M), HLA-G heavy chain fused to B2M and to the Fc portion of an immunoglobulin, and HLA-G alpha-1 domain either fused to the Fc part of an immunoglobulin or as a synthetic peptide. Our results demonstrate the tolerogenic function of B2M-HLA-G fusion proteins, and especially of B2M-HLA-G5, which were capable of significantly delaying allogeneic skin graft rejection in a murine in vivo transplantation model. The results from our studies suggest that HLA-G recombinant proteins are relevant candidates for tolerance induction in human transplantation.

Original languageEnglish (US)
Article numbere21011
JournalPloS one
Issue number7
StatePublished - Jul 19 2011


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

Cite this

Favier, B., HoWangYin, K. Y., Wu, J., Caumartin, J., Daouya, M., Horuzsko, A., Carosella, E. D., & Le Maoult, J. (2011). Tolerogenic function of dimeric forms of HLA-g recombinant proteins: A comparative study in Vivo. PloS one, 6(7), [e21011].