Evaluation of human and non-human primate antibody binding to pig cells lacking GGTA1/CMAH/β4GalNT2 genes

Xenotransplantation
Jose L EstradaJoseph Tector

Abstract

Simultaneous inactivation of pig GGTA1 and CMAH genes eliminates carbohydrate xenoantigens recognized by human antibodies. The β4GalNT2 glycosyltransferase may also synthesize xenoantigens. To further characterize glycan-based species incompatibilities, we examined human and non-human primate antibody binding to cells derived from genetically modified pigs lacking these carbohydrate-modifying genes. The Cas9 endonuclease and gRNA were used to create pigs lacking GGTA1, GGTA1/CMAH, or GGTA1/CMAH/β4GalNT2 genes. Peripheral blood mononuclear cells were isolated from these animals and examined for binding to IgM and IgG from humans, rhesus macaques, and baboons. Cells from GGTA1/CMAH/β4GalNT2 deficient pigs exhibited reduced human IgM and IgG binding compared to cells lacking both GGTA1 and CMAH. Non-human primate antibody reactivity with cells from the various pigs exhibited a slightly different pattern of reactivity than that seen in humans. Simultaneous inactivation of the GGTA1 and CMAH genes increased non-human primate antibody binding compared to cells lacking either GGTA1 only or to those deficient in GGTA1/CMAH/β4GalNT2. Inactivation of the β4GalNT2 gene reduces human and non-human primate antibody binding resulting in dimi...Continue Reading

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Citations

Nov 10, 2015·Expert Review of Clinical Immunology·David Kc Cooper, Rita Bottino
Feb 26, 2016·Transplantation·Zheng-Yu WangA Joseph Tector
Jan 28, 2016·Xenotransplantation·David K C CooperRita Bottino
Sep 15, 2015·The Journal of Pathology·David K C CooperDavid Ayares
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