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9 results on '"Sijts, Alice"'

1. Human milk extracellular vesicles target nodes in interconnected signalling pathways that enhance oral epithelial barrier function and dampen immune responses

Author

Zonneveld, Marijke I., primary, Herwijnen, Martijn J.C., additional, Fernandez‐Gutierrez, Marcela M., additional, Giovanazzi, Alberta, additional, Groot, Anne Marit, additional, Kleinjan, Marije, additional, Capel, Toni M.M., additional, Sijts, Alice J.A.M., additional, Taams, Leonie S., additional, Garssen, Johan, additional, Jong, Esther C., additional, Kleerebezem, Michiel, additional, Nolte‐’t Hoen, Esther N.M., additional, Redegeld, Frank A., additional, and Wauben, Marca H.M., additional

Published
2021
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2. CD8+T cells ofListeria monocytogenes-infected mice recognize both linear and spliced proteasome products

Author

Platteel, Anouk C M, Mishto, Michele, Textoris-Taube, Kathrin, Keller, Christin, Liepe, Juliane, Busch, Dirk H, Kloetzel, Peter M, Sijts, Alice J A M, LS Immunologie, and dI&I RA-I&I I&I

Subjects
0301 basic medicine, Proteasome Endopeptidase Complex, Immunology, Antigen presentation, Epitopes, T-Lymphocyte, CD8-Positive T-Lymphocytes, CD8+ T cells, Major histocompatibility complex, Mass Spectrometry, Epitope, Mice, 03 medical and health sciences, 0302 clinical medicine, Antigen, MHC class I, Animals, Protein Splicing, Immunology and Allergy, Cytotoxic T cell, Computer Simulation, Listeriosis, Immune Evasion, Antigen Presentation, Proteasome, biology, Linear epitope, Histocompatibility Antigens Class I, MHC class I antigen processing, Listeria monocytogenes, Molecular biology, Tumor antigen, 030104 developmental biology, biology.protein, Peptides, Proteasome-catalyzed peptide splicing, 030215 immunology
Abstract

CD8(+) T cells responding to infection recognize pathogen-derived epitopes presented by MHC class-I molecules. While most of such epitopes are generated by proteasome-mediated antigen cleavage, analysis of tumor antigen processing has revealed that epitopes may also derive from proteasome-catalyzed peptide splicing (PCPS). To determine whether PCPS contributes to epitope processing during infection, we analyzed the fragments produced by purified proteasomes from a Listeria monocytogenes polypeptide. Mass spectrometry identified a known H-2K(b) -presented linear epitope (LLO296-304 ) in the digests, as well as four spliced peptides that were trimmed by ERAP into peptides with in silico predicted H-2K(b) binding affinity. These spliced peptides, which displayed sequence similarity with LLO296-304 , bound to H-2K(b) molecules in cellular assays and one of the peptides was recognized by CD8(+) T cells of infected mice. This spliced epitope differed by one amino acid from LLO296-304 and double staining with LLO296-304 - and spliced peptide-folded MHC multimers showed that LLO296-304 and its spliced variant were recognized by the same CD8(+) T cells. Thus, PCPS multiplies the variety of peptides that is processed from an antigen and leads to the production of epitope variants that can be recognized by cross-reacting pathogen-specific CD8(+) T cells. Such mechanism may reduce the chances for pathogen immune evasion. This article is protected by copyright. All rights reserved.

Published
2016

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