Identification of B cell epitopes enhanced by protein unfolding and aggregation.


Journal

Molecular immunology
ISSN: 1872-9142
Titre abrégé: Mol Immunol
Pays: England
ID NLM: 7905289

Informations de publication

Date de publication:
01 2019
Historique:
received: 26 07 2018
revised: 16 10 2018
accepted: 30 11 2018
pubmed: 15 12 2018
medline: 1 5 2019
entrez: 15 12 2018
Statut: ppublish

Résumé

Aggregation of therapeutic proteins is a key factor in the generation of unwanted immunogenicity, and can result in reduced serum half-life, neutralization of function and adverse health effects. There is currently little information regarding how aggregates interact with B-cell receptors or cognate antibodies at the protein sequence level, or whether non-native, aggregate-induced epitopes predominate in these interactions. Using an antibody fragment (single chain antibody variable fragment; scFv) that forms aggregates readily at low temperature, anti-scFv IgG antibody responses were generated by intraperitoneal injection of BALB/c strain mice with monomer or aggregate preparations. Aggregate-specific immunosignatures were identified by oligo-peptide microarray fine epitope mapping, using overlapping 15mer peptides based on the linear sequence of scFv, printed onto glass slides. IgG antibodies from mice immunized with aggregated scFv preferentially recognized a patch of overlapping peptides. This region mapped to a β-strand located at the interface between the V

Identifiants

pubmed: 30550980
pii: S0161-5890(18)30518-2
doi: 10.1016/j.molimm.2018.11.020
pmc: PMC6344229
pii:
doi:

Substances chimiques

Epitopes, B-Lymphocyte 0
Immunoglobulin G 0
Protein Aggregates 0
Single-Chain Antibodies 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

181-189

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 105610/Z/14/Z
Pays : United Kingdom

Informations de copyright

Copyright © 2018 The Authors. Published by Elsevier Ltd.. All rights reserved.

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Auteurs

Timothy J Eyes (TJ)

Lydia Becker Institute of Immunology and Inflammation, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Oxford Road, Manchester, UK.

James I Austerberry (JI)

Lydia Becker Institute of Immunology and Inflammation, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Oxford Road, Manchester, UK.

Rebecca J Dearman (RJ)

Lydia Becker Institute of Immunology and Inflammation, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Oxford Road, Manchester, UK.

Linus O Johannissen (LO)

Faculty of Science and Engineering, Manchester Institute of Biotechnology, The University of Manchester, Princess Street, Manchester, UK.

Ian Kimber (I)

Lydia Becker Institute of Immunology and Inflammation, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Oxford Road, Manchester, UK.

Noel Smith (N)

Lonza, Granta Park, Cambridge, UK.

Angela Thistlethwaite (A)

Lydia Becker Institute of Immunology and Inflammation, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Oxford Road, Manchester, UK.

Jeremy P Derrick (JP)

Lydia Becker Institute of Immunology and Inflammation, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Oxford Road, Manchester, UK. Electronic address: Jeremy.Derrick@manchester.ac.uk.

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