Immunological property of antibodies against N-glycolylneuraminic acid epitopes in cytidine monophospho-N-acetylneuraminic acid hydroxylase-deficient mice

J Immunol. 2010 Mar 15;184(6):3269-75. doi: 10.4049/jimmunol.0902857. Epub 2010 Feb 19.

Abstract

The generation of pigs devoid of Galalpha1,3Galbeta1,4GlcNAc (Gal) residues has stimulated interest in non-Gal Ags as potentially important targets for Ab binding leading to rejection of pig organ xenografts in humans. Although N-glycolylneuraminic acid (NeuGc) epitopes, which are widely expressed on the endothelial cells of all mammals except humans, are likely targets of anti-non-Gal Abs, this aspect has not been investigated intensively owing to the absence of an appropriate animal model. In this study, we used CMAH(-/-) mice, which are completely deficient in NeuGc and thus produce anti-NeuGc Abs. Sera obtained from CMAH(-/-) mice and healthy human volunteers having anti-NeuGc Abs initiated complement-mediated lysis against CMAH(+/+) cells in vitro. The cytotoxic activity of anti-NeuGc Abs was also determined in vivo (i.e., NeuGc-expressing CMAH(+/+) mouse splenocytes that had been i.v. injected were completely eliminated in syngeneic CMAH(-/-) mice). CMAH(-/-) mice rejected the islets transplanted from syngeneic CMAH(+/+) mice. Thus, the anti-NeuGc Ab-mediated response may be crucially involved in xenograft loss. This is the first direct demonstration of the immunogenic property of NeuGc determinants as targets of the corresponding Abs in CMAH(+/+)-to-CMAH(-/-) transplantation setting.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies / toxicity*
  • Binding Sites, Antibody
  • Cytotoxicity Tests, Immunologic*
  • Diabetes Mellitus, Experimental / immunology
  • Endothelium, Vascular / immunology
  • Endothelium, Vascular / metabolism
  • Epitopes / biosynthesis
  • Epitopes / immunology*
  • Female
  • Galactosyltransferases / deficiency
  • Galactosyltransferases / genetics
  • Graft Rejection / immunology
  • Heart Transplantation / immunology
  • Humans
  • Immunoglobulin G / toxicity
  • Immunoglobulin M / toxicity
  • Islets of Langerhans Transplantation / immunology
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Mixed Function Oxygenases / deficiency*
  • Mixed Function Oxygenases / genetics*
  • Neuraminic Acids / immunology*
  • Neuraminic Acids / metabolism
  • Rats
  • Rats, Inbred F344
  • Swine
  • Transplantation, Heterologous

Substances

  • Antibodies
  • Epitopes
  • Immunoglobulin G
  • Immunoglobulin M
  • Neuraminic Acids
  • N-glycolylneuraminic acid
  • Mixed Function Oxygenases
  • CMPacetylneuraminate monooxygenase
  • Galactosyltransferases