glyXera is pleased to announce that a successful collaboration with Hannover Medical School resulted in publishing an article in Xenotransplantation titled “Genetic knockout of porcine GGTA1 or CMAH/GGTA1 is associated with the emergence of neo-glycans“.
Pig-derived tissues could overcome the shortage of human donor organs in transplantation. The most profound barrier to pig-to-human xenotransplantation is the immunological rejection of the organ graft. Recognition of a pig tissue as non-self in humans is related to specific carbohydrate antigens that are not present on human glycoproteins and glycolipids and can trigger an adverse immune response. For example, glycans with terminal α-galactose (α-Gal) and N-glycolylneuraminic acid (NGNA), which are synthesized by enzymes encoded by the genes GGTA1 and CMAH, are known to play a major role in immunogenicity of porcine tissue. In a major milestone toward long-term survival of porcine xenografts, the genes GGTA1 and CMAH were knocked out. Although promising, many challenges still lie ahead before the therapeutic potential of this approach can be fully recognized. Importantly, to create safe tissues completely depleted of immunogenic epitopes, a detailed and sensitive analysis of glycosylation is of prerequisite.
This study investigated the effects of genetic knockout of two important glycan epitopes on the porcine glycome. By using glyXera’s patented glyXboxCE technology, N-glycosylation and glycosphingolipid glycosylation of porcine pericardium was interrogated, focusing on the potential emergence of neo-glycoepitopes that might act as novel xenogeneic antigens. Structural characterization of glycans will provide significant information to clinical studies regarding immune rejection responses induced by carbohydrate antigens during xenotransplantation. Therefore, glycan analysis can aid the development of animal tissues and organs that are suitable for transplantation in humans.
glyXera’s contribution to this study included:
- Data processing using glyXtoolCE data analysis tool including integrated database lookup
- Identification of unknown peaks as labeling intermediates
- Utilization of different exoglycosidase enzymes in glycan characterization
For more information about this article please visit the publication web page: https://onlinelibrary.wiley.com/doi/10.1111/xen.12804