Leviatan Ben-Arye, Shani; Schneider, Christoph; Yu, Hai; Bashir, Salam; Chen, Xi; von Gunten, Stephan; Padler-Karavani, Vered (2019). Differential Recognition of Diet-Derived Neu5Gc-Neoantigens on Glycan Microarrays by Carbohydrate-Specific Pooled Human IgG and IgA Antibodies. Bioconjugate chemistry, 30(5), pp. 1565-1574. American Chemical Society 10.1021/acs.bioconjchem.9b00273
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VonGunten_Differential Recognition of Diet-Derived Neu5Gc-Neoantigens onGlycan Microarrays.pdf - Published Version Restricted to registered users only Available under License Publisher holds Copyright. Download (2MB) | Request a copy |
Sialic acids (Sias) cover vertebrate cell surface glycans. N-Acetylneuraminic acid (Neu5Ac) and its hydroxylated form N-glycolylneuraminic acid (Neu5Gc) are common Sia in mammals. Humans cannot synthesize Neu5Gc but accumulate it on cells through red-meat rich diets, generating numerous immunogenic Neu5Gc-neoantigens. Consequently, humans have diverse anti-Neu5Gc antibodies affecting xenotransplantation, cancer, atherosclerosis, and infertility. Anti-Neu5Gc antibodies circulate as IgG, IgM, and IgA isotypes; however, repertoires of the different isotypes in a large population have not been studied yet. Here, we used glycan microarrays to investigate anti-Neu5Gc IgGs and IgAs in intravenous immunoglobulin (IVIG) or pooled human IgA, respectively. Binding patterns on microarrays fabricated with Neu5Gc- and Neu5Ac-glycans, together with inhibition assays, revealed that different IVIG preparations have highly specific anti-Neu5Gc IgG reactivity with closely related repertoires, while IgAs show cross-reactivity against several Neu5Ac-glycans. Such different anti-Neu5Gc IgG/IgA repertoires in individuals could possibly mediate distinctive effects on human diseases.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Pharmacology |
UniBE Contributor: |
von Gunten, Stephan |
Subjects: |
600 Technology > 610 Medicine & health |
ISSN: |
1043-1802 |
Publisher: |
American Chemical Society |
Language: |
English |
Submitter: |
Celine Joray |
Date Deposited: |
15 Jul 2019 15:22 |
Last Modified: |
05 Dec 2022 15:28 |
Publisher DOI: |
10.1021/acs.bioconjchem.9b00273 |
PubMed ID: |
30994337 |
BORIS DOI: |
10.7892/boris.130510 |
URI: |
https://boris.unibe.ch/id/eprint/130510 |
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