Differential Recognition of Diet-Derived Neu5Gc-Neoantigens on Glycan Microarrays by Carbohydrate-Specific Pooled Human IgG and IgA Antibodies.

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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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:

01 Dec 2020 15:51

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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