Cited by 29Advanced Proteomics Techniques and ApplicationsXenotransplantation and immune responsevaccines and immunoinformatics approaches

Antigenicity of Bovine Pericardium Determined by a Novel Immunoproteomic Approach

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Gates, Katherine V., Dalgliesh, Ailsa J., Griffiths, Leigh G.·2017·Scientific Reports

Abstract

Despite bovine pericardium (BP) being the primary biomaterial used in heart valve bioprostheses, recipient graft-specific immune responses remain a significant cause of graft failure. Consequently, tissue antigenicity remains the principal barrier for expanding use of such biomaterials in clinical practice. We hypothesize that our understanding of BP antigenicity can be improved by application of a combined affinity chromatography shotgun immunoproteomic approach to identify antigens that have previously been overlooked. Liquid Chromatography Tandem Mass Spectrometry (LC-MS/MS) analysis of affinity chromatography purified antigens resulted in identification of 133 antigens. Most importantly, antigens were identified from all subcellular locations, including 18 integral membrane protein antigens. Critically, isoforms of several protein families were found to be antigenic suggesting the possibility that shared epitope domains may exist. Furthermore, proteins associated with immune, coagulation, and inflammatory pathways were over-represented, suggesting that these biological processes play a key role in antigenicity. This study brings to light important determinants of antigenicity in a clinically relevant xenogeneic biomaterial (i.e. BP) and further validates a rapid, high-throughput method for immunoproteomic antigen identification.

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  • The heterogeneous results of some decellularization protocols in removing immunogenic factors make robust antigen removal steps necessary to overcome immunogenicity.

    “The heterogeneous results of some decellularization protocols in removing immunogenic factors make applying robust antigen removal steps necessary to overcome the immunogenicity issue [184].”

    From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [184]

    The Introduction (page not provided) says decellularized tissue can retain antigens that provoke graft-specific immune responses, and the Discussion argues for a move from merely decellularized to antigen-removed tissues. The paper does not establish that different decellularization protocols produce heterogeneous antigen-removal results. (LLM, conf=0.85)

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Cited by

Sorted by citations

Authors
Gates, K. V., Dalgliesh, A. J., & Griffiths, L. G.
Affiliations
Mayo Clinic (US)
Corresponding author
Griffiths, Leigh G.
Venue
Scientific Reports
Published
2017-05-26
Volume
7
Issue
1
Pages
2446-2446
ISSN
2045-2322 (ISSN-L)
OpenAlex
W2620363728
Cited by
29
References
3
Citations by year
2025: 4 · 2024: 2 · 2023: 5 · 2022: 1 · 2021: 3 · 2020: 6 · 2019: 4 · 2018: 3 · 2017: 1
FWCI
1.89
Type
journal article
Language
en
Open access
Locations
  • Scientific Reports (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Institutes of Health (T32OD010931, T35OD010956)
  • University of California, Davis
  • National Heart, Lung, and Blood Institute (R01HL115205)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Health Sciences › Medicine › Surgery › Xenotransplantation and immune response
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Keywords
bovine pericardium, antigenicity, xenograft rejection, immunoproteomics, affinity chromatography, membrane proteins, protein isoforms, shared epitope, coagulation factors, inflammatory proteins
MeSH terms
Animals, Epitopes, Antigens, Biocompatible Materials, Cattle, Chromatography, Liquid, Pericardium, Proteome, Tissue Engineering, Proteomics, Tandem Mass Spectrometry

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