Autoantibody and T cell responses to oxidative post-translationally modified insulin neoantigenic peptides in type 1 diabetes.

Autoimmunity Immune response Insulin Insulin autoantibodies Insulin neoepitope peptide Neoantigen Neoepitope Oxidative post-translational modifications Post-translational modifications

Journal

Diabetologia
ISSN: 1432-0428
Titre abrégé: Diabetologia
Pays: Germany
ID NLM: 0006777

Informations de publication

Date de publication:
01 2023
Historique:
received: 28 04 2022
accepted: 28 07 2022
pubmed: 8 10 2022
medline: 15 12 2022
entrez: 7 10 2022
Statut: ppublish

Résumé

Antibodies specific to oxidative post-translational modifications (oxPTM) of insulin (oxPTM-INS) are present in most individuals with type 1 diabetes, even before the clinical onset. However, the antigenic determinants of such response are still unknown. In this study, we investigated the antibody response to oxPTM-INS neoepitope peptides (oxPTM-INSPs) and evaluated their ability to stimulate humoral and T cell responses in type 1 diabetes. We also assessed the concordance between antibody and T cell responses to the oxPTM-INS neoantigenic peptides. oxPTM-INS was generated by exposing insulin to various reactive oxidants. The insulin fragments resulting from oxPTM were fractionated by size-exclusion chromatography further to ELISA and LC-MS/MS analysis to identify the oxidised peptide neoepitopes. Immunogenic peptide candidates were produced and then modified in house or designed to incorporate in silico-oxidised amino acids during synthesis. Autoantibodies to the oxPTM-INSPs were tested by ELISA using sera from 63 participants with new-onset type 1 diabetes and 30 control participants. An additional 18 fresh blood samples from participants with recently diagnosed type 1 diabetes, five with established disease, and from 11 control participants were used to evaluate, in parallel, CD4 We observed antibody and T cell responses to three out of six LC-MS/MS-identified insulin peptide candidates: A:12-21 (SLYQLENYCN, native insulin peptide 3 [Nt-INSP-3]), B:11-30 (LVEALYLVCGERGFFYTPKT, Nt-INSP-4) and B:21-30 (ERGFFYTPKT, Nt-INSP-6). For Nt-INSP-4 and Nt-INSP-6, serum antibody binding was stronger in type 1 diabetes compared with healthy control participants (p≤0.02), with oxidised forms of ERGFFYTPKT, oxPTM-INSP-6 conferring the highest antibody binding (83% binders to peptide modified in house by hydroxyl radical [ Our findings support the concept that oxidative stress, and neoantigenic epitopes of insulin, may be involved in the immunopathogenesis of type 1 diabetes.

Identifiants

pubmed: 36207582
doi: 10.1007/s00125-022-05812-4
pii: 10.1007/s00125-022-05812-4
pmc: PMC9729141
doi:

Substances chimiques

Insulin 0
Autoantibodies 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

132-146

Subventions

Organisme : NCATS NIH HHS
ID : UL1 TR001863
Pays : United States

Informations de copyright

© 2022. The Author(s).

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Auteurs

Rocky Strollo (R)

Department of Science and Technology for Humans and the Environment, Università Campus Bio-Medico di Roma, Rome, Italy.

Chiara Vinci (C)

Biochemical Pharmacology, William Harvey Research Institute, Queen Mary University of London, London, UK.

Y K Stella Man (YKS)

Biochemical Pharmacology, William Harvey Research Institute, Queen Mary University of London, London, UK.

Sara Bruzzaniti (S)

Institute for Experimental Endocrinology and Oncology 'G. Salvatore', Consiglio Nazionale delle Ricerche, Naples, Italy.
Department of Biology, Università degli Studi di Napoli 'Federico II', Naples, Italy.

Erica Piemonte (E)

Department of Molecular Medicine and Medical Biotechnology, Università degli Studi di Napoli 'Federico II', Naples, Italy.

Ghadeer Alhamar (G)

Department of Medicine, Unit of Endocrinology & Diabetes, Università Campus Bio-Medico di Roma, Rome, Italy.

Silvia Irina Briganti (SI)

Department of Medicine, Unit of Endocrinology & Diabetes, Università Campus Bio-Medico di Roma, Rome, Italy.

Ilaria Malandrucco (I)

The UOSD of Endocrinology and Metabolic Diseases, Azienda Sanitaria Locale (ASL) Frosinone, Frosinone, Italy.

Flavia Tramontana (F)

Department of Medicine, Unit of Endocrinology & Diabetes, Università Campus Bio-Medico di Roma, Rome, Italy.

Chiara Fanali (C)

Department of Science and Technology for Humans and the Environment, Università Campus Bio-Medico di Roma, Rome, Italy.

James Garnett (J)

Centre for Host-Microbiome Interactions, Dental Institute, King's College London, London, UK.
School of Biological and Chemical Sciences, Queen Mary University of London, London, UK.

Roberto Buccafusca (R)

School of Biological and Chemical Sciences, Queen Mary University of London, London, UK.

Perrin Guyer (P)

Program for Translational Immunology, Benaroya Research Institute, Seattle, WA, USA.

Mark Mamula (M)

Department of Medicine, Yale University School of Medicine, New Haven, CT, USA.

Eddie A James (EA)

Program for Translational Immunology, Benaroya Research Institute, Seattle, WA, USA.

Paolo Pozzilli (P)

Department of Medicine, Unit of Endocrinology & Diabetes, Università Campus Bio-Medico di Roma, Rome, Italy.

Johnny Ludvigsson (J)

Division of Pediatrics, Department of Biomedical and Clinical Sciences, Crown Princess Victoria Children's Hospital, Linköping University, Linköping, Sweden.

Paul G Winyard (PG)

Institute of Biomedical and Clinical Science, University of Exeter Medical School, St Luke's Campus, Exeter, UK.

Mario Galgani (M)

Institute for Experimental Endocrinology and Oncology 'G. Salvatore', Consiglio Nazionale delle Ricerche, Naples, Italy.
Department of Molecular Medicine and Medical Biotechnology, Università degli Studi di Napoli 'Federico II', Naples, Italy.

Ahuva Nissim (A)

Biochemical Pharmacology, William Harvey Research Institute, Queen Mary University of London, London, UK. a.nissim@qmul.ac.uk.

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