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Home / Equine Research Bank / Glycoconj J / Identification by mass spectrometry and immunoblotting of xe...
Glycoconjugate journal2020; 37(4); 485-498; doi: 10.1007/s10719-020-09931-1

Identification by mass spectrometry and immunoblotting of xenogeneic antigens in the N- and O-glycomes of porcine, bovine and equine heart tissues.

Abstract: 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 α-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 and O-glycans by β-elimination. Released oligosaccharides were analyzed by liquid chromatography - tandem mass spectrometry. In total, 102 N-glycans and 40 O-glycans were identified in animal heart tissue lysates. The N- and O-glycan patterns were different between species. α-Gal and Neu5Gc were identified on both N- and O-linked glycans, N,N´-diacetyllactosamine (LacdiNAc) on N-glycans only and sulfated O-glycans. The relative amounts of α-Gal-containing N-glycans were higher in bovine compared to equine and porcine pericardia. In contrast to the restricted number of proteins carrying α-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-sialylated O-glycans, and bovine pericardium the highest level of Neu5Gc-sialylated N-glycans. The identified N- and O-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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Publication Date: 2020-06-15 PubMed ID: 32542517PubMed Central: PMC7329767DOI: 10.1007/s10719-020-09931-1Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research examines the antigens found in the tissues of pigs, cows, and horses that are used in the production of animal bioprosthetic heart valves (BHV). The results reveal a variety of N- and O-linked glycans which could potentially trigger patient immune reactions, as well as varying expression of these potential target antigens between species and tissues.

Introduction and Objectives

  • This study aims to investigate the expression of potential immune target antigens in tissues used for the production of animal bioprosthetic heart valves (BHV). Particularly, the research focuses on antigens such as α-Gal and Neu5Gc, whose response in recipients of these valves, especially the young ones, may cause a structural deterioration of the valve.

Methodology

  • Protein lysates or cellular extracts were taken from the aortic and pulmonary valves of pigs, and from the pericardia of pigs, cows, and horses. These extracts were analyzed using Western blotting, a molecular biology technique for detecting specific proteins.
  • The existing N-glycans in the lysates were released by an enzyme called PNGase F. O-glycans were released by a process called β-elimination.
  • The resulting free oligosaccharides were analyzed using liquid chromatography – tandem mass spectrometry.

Findings

  • The researchers identified a total of 102 N-glycans and 40 O-glycans in the animal heart tissue lysates. They found that the patterns of these complex sugars were different across species.
  • Antigens α-Gal and Neu5Gc were detected on both N- and O-linked glycans.
  • The distribution of proteins carrying Neu5Gc varied between species and even between different tissues within the same species, while the number of proteins with α-Gal and N,N´-diacetyllactosamine (LacdiNAc) was constant.
  • The quantity of α-Gal sugars was higher in bovine pericardia than in those of horses or pigs.
  • Pig pericardium displayed the highest levels of Neu5Gc-sialylated O-glycans, with bovine pericardium carrying the most Neu5Gc-sialylated N-glycans.

Conclusion and Future Directions

  • The researchers have identified a list of N- and O-linked glycans present in the heart tissues of the animals used for BHV, some of which might be immunogenic, potentially stimulating an immune response in humans.
  • This information could guide future genetic engineering efforts with the goal of preventing the expression of these glycans, thereby rendering these tissues less likely to trigger an immune response in humans.

Cite This Article

APA
Jin C, Cherian RM, Liu J, Playà-Albinyana H, Galli C, Karlsson NG, Breimer ME, Holgersson J. (2020). Identification by mass spectrometry and immunoblotting of xenogeneic antigens in the N- and O-glycomes of porcine, bovine and equine heart tissues. Glycoconj J, 37(4), 485-498. https://doi.org/10.1007/s10719-020-09931-1

Publication

Glycoconjugate journal
ISSN: 1573-4986
NlmUniqueID: 8603310
Country: United States
Language: English
Volume: 37
Issue: 4
Pages: 485-498

Researcher Affiliations

Jin, Chunsheng
  • Department of Medical Biochemistry, Institute of Biomedicine Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden. chunsheng.jin@medkem.gu.se.
Cherian, Reeja Maria
  • Department of Surgery, Institute of Clinical Sciences, Sahlgrenska Academy at University of Gothenburg, Göteborg, Sweden.
Liu, Jining
  • Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Playà-Albinyana, Heribert
  • Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Department of Biochemistry and Biotechnology, Faculty of Chemistry, Rovira i Virgili University, Tarragona, Spain.
Galli, Cesare
  • Avantea Laboratory of Reproductive Technologies, Cremona, Italy.
  • Avantea Foundation, Cremona, Italy.
Karlsson, Niclas G
  • Department of Medical Biochemistry, Institute of Biomedicine Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Breimer, Michael E
  • Department of Surgery, Institute of Clinical Sciences, Sahlgrenska Academy at University of Gothenburg, Göteborg, Sweden.
Holgersson, Jan
  • Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.

MeSH Terms

  • Animals
  • Antigens, Heterophile / analysis
  • Antigens, Heterophile / immunology
  • Antigens, Heterophile / metabolism
  • Aortic Valve / metabolism
  • Cattle
  • Horses
  • Immunoblotting
  • Lewis Blood Group Antigens / metabolism
  • Myocardium / metabolism
  • Pericardium / metabolism
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism
  • Pulmonary Valve / metabolism
  • Swine
  • Tandem Mass Spectrometry

Conflict of Interest Statement

The authors declare that they have no conflict of interest.

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