Page 268 - ebook

[E. Immunology] E-3

Diversity of Non-human Glycan Antigen Expression in

Porcine as Xenograft Model

Ji Eun Park¹,², Myung Jin Oh¹,², Hyun Joo An¹,²*

¹Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, Korea,

²Asia-Pacific Glycomics Reference Site, Asia-Pacific Glycomics Reference Site, Daejeon 34134, Korea

Xenotransplantation is a solution to bridge the gap between patients with severe organ failures and donors, but

differences in glycosylation between humans and porcine act as an immune barrier. Recent studies have shown that
representative non-human glycan moieties such as galactose-α1,3-galactose(α-gal), NeuGc, and SDa antigens act

as epitopes triggering antibody-mediated rejection (AMR). Interestingly, unlike other transferases of non-human
antigen expressed only in porcine, SDa antigen glycans can be found in both porcine and humans. Therefore, a

structural approach is needed to define the xenoantigen characteristics. Here, we performed glycan profiling and
structural analysis of non-human moieties in porcine endothelial cells and serum, peripheral blood mononuclear

cells(PBMCs). We identify various glycan isomers and heterogeneity characteristics by accurate masses, retention
times, LC/MS/MS, and glycan sequencing. NeuAc-sialylated glycans were observed in serum and cells as major

components, whereas NeuGc-sialylated glycans were major components in PBMCs. Using MS/MS spectra, unique
glycosylation of sialic acid attached to antennal N-acetyl glucosamine was determined in cells, and glycans

expressing both SDa antigen and α-gal epitope were identified in PBMCs. Our structural profiling data of non-
human glycans will be a valuable reference for immune response studies based on various structural features of
xeno-glycan antigens in mammals.