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Identification by mass spectrometry and immunoblotting of xenogeneic antigens in theN- andO-glycomes of porcine, bovine and equine heart tissues

Journal article
Authors Chunsheng Jin
Reeja Maria Cherian
Jining Liu
Heribert Playà-Albinyana
C. Galli
Niclas G. Karlsson
Michael Breimer
Jan Holgersson
Published in Glycoconjugate Journal
Volume 37
Pages 485-498
ISSN 0282-0080
Publication year 2020
Published at Institute of Clinical Sciences, Department of Surgery
Institute of Biomedicine
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 485-498
Language en
Keywords Bioprosthetic heart valves, structural valve deterioration, glycome, xenogeneic antigen, liquid chromatography - tandem mass spectrometry, o-linked oligosaccharides, alpha-gal epitope, genetic-modification, forssman antigen, valves, glycans, mucin, antibody, expression, pigs, Biochemistry & Molecular Biology
Subject categories Clinical Medicine


Animal bioprosthetic heart valves (BHV) are used to replace defective valves in patients with valvular heart disease. Especially young BHV recipients may experience a structural valve deterioration caused by an immune reaction in which alpha-Gal and Neu5Gc are potential target antigens. The expression of these and other carbohydrate antigens in animal tissues used for production of BHV was explored. Protein lysates of porcine aortic and pulmonary valves, and porcine, bovine and equine pericardia were analyzed by Western blotting using anti-carbohydrate antibodies and lectins.N-glycans were released by PNGase F digestion andO-glycans by beta-elimination. Released oligosaccharides were analyzed by liquid chromatography - tandem mass spectrometry. In total, 102N-glycans and 40O-glycans were identified in animal heart tissue lysates. TheN- andO-glycan patterns were different between species. alpha-Gal and Neu5Gc were identified on bothN- andO-linked glycans,N,N '-diacetyllactosamine (LacdiNAc) onN-glycans only and sulfatedO-glycans. The relative amounts of alpha-Gal-containingN-glycans were higher in bovine compared to equine and porcine pericardia. In contrast to the restricted number of proteins carrying alpha-Gal and LacdiNAc, the distribution of proteins carrying Neu5Gc-determinants varied between species and between different tissues of the same species. Porcine pericardium carried the highest level of Neu5Gc-sialylatedO-glycans, and bovine pericardium the highest level of Neu5Gc-sialylatedN-glycans. The identifiedN-andO-linked glycans, some of which may be immunogenic and remain in BHVs manufactured for clinical use, could direct future genetic engineering to prevent glycan expression rendering the donor tissues less immunogenic in humans.

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