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Egg Allergy
Published in Andreas L. Lopata, Food Allergy, 2017
Paul J. Turner, Dianne E. Campbell
Ovomucoid (Gal d 1) is the second most abundant glycoprotein by weight, and may be the dominant allergen in IgE-mediated egg allergy, primarily due to the resistance of its IgE-binding epitopes to heat and digestion (Urisu et al. 1997). However, ovomucoid does undergo a degree of gastric-modification, which affects allergenicity; it has been suggested that this observation might explain the phenomenon of contact reactions to raw egg in children who otherwise tolerate egg ingestion (Urisu et al. 1997). Ovomucoid comprises 186 amino acids arranged in three tandem domains (Gal d 1.1, 1.2, and 1.3), the second of which may be most associated with IgE binding (Cooke and Sampson 1997). A number of studies have reported IgE to ovomucoid is predictive for lack of tolerance to heat-modified egg (Ando et al. 2008, Lemon-Mule et al. 2008, Tan et al. 2013) and persistence of egg allergy (Bernhisel-Broadbent et al. 1994, Jarvinen et al. 2007). Epitope mapping, using a peptide microarray immunoassay, has been used to study IgE-binding to ovomucoid; interestingly, sera from 17 of 50 patients studied did not demonstrate IgE binding to linear epitopes (Martinez-Botas et al. 2013).
Beyond the amyloid hypothesis: how current research implicates autoimmunity in Alzheimer’s disease pathogenesis
Published in Critical Reviews in Clinical Laboratory Sciences, 2023
Miyo K. Chatanaka, Dorsa Sohaei, Eleftherios P. Diamandis, Ioannis Prassas
Sim et al. used a high throughput screening method based on random peptide microarrays of 29,240 unbiased peptides in 19 AD and 19 non-demented age-matched all-female plasma samples [328]. The team identified 110 candidate antibody-binding targets that were upregulated, and 30 that were downregulated. In addition, hierarchical clustering analysis of the selected peptides showed that only the upregulated IgG and IgM could categorically divide the two groups. Some of these target proteins are SOS1, TNFRSF21, ATM, and S100A1 (recognized by IgG upregulation), SOS1 and SP4 (recognized by IgM upregulation), and GNPAT and CNTN2 (recognized by IgM downregulation). Due to the large number of proteins identified, these autoantibodies will not be summarized in Table 1. The full list of proteins/autoantibodies is described by Sim et al. [328].
The interdependence of machine learning and LC-MS approaches for an unbiased understanding of the cellular immunopeptidome
Published in Expert Review of Proteomics, 2022
Morten Nielsen, Nicola Ternette, Carolina Barra
Given the essential role of MHC in defining the targets of T cell immunity, large efforts have been dedicated to understanding the rules of MHC antigen binding and presentation, and to the development of experimental and computational techniques for improved characterization, and identification of immunopeptidomes. The experimental techniques include binding affinity [2] and binding stability [3] assays, and peptide-microarrays [4,5]. All of these techniques rely on investigating the effect of in vitro binding of individually synthetically synthesized peptides (many thousands in the case of peptide-microarrays), and hence, they all ignore many important aspects of the biologically relevant antigen processing and presentation pathway. An alternative experimental technique first applied in the 1990th, is liquid chromatography-tandem mass spectrometry (LC-MS/MS) where several thousands of natural HLA presented peptides are detected in a single experiment [6]. Such MS HLA eluted peptides hold information related to the natural steps of the HLA antigen processing and presentation pathway, and have been demonstrated to be a rich source of information both for the identification of HLA antigens in the context of a given pathogen/disease and for learning the patterns of and training prediction model for HLA antigen presentation (reviewed in [7]).
Membrane-binding peptides for extracellular vesicles on-chip analysis
Published in Journal of Extracellular Vesicles, 2020
Alessandro Gori, Alessandro Romanato, Greta Bergamaschi, Alessandro Strada, Paola Gagni, Roberto Frigerio, Dario Brambilla, Riccardo Vago, Silvia Galbiati, Silvia Picciolini, Marzia Bedoni, George G. Daaboul, Marcella Chiari, Marina Cretich
Most importantly, the size dependency of captured EV showed that BP peptides have preferential affinity towards vesicles in the 50–150 nm size (sEV), as we demonstrated by using either synthetic liposomes of different sizes (150–400 nm range) and by using EV obtained from samples enriched with sEVs or MVs (different UC fractions). These pieces of evidence are in full agreement with previous reports on the striking size selectivity that curvature-sensing peptides are able to display [16,17,20,41]. The combined efficiency and selectivity of sEV binding were also demonstrated by the on-chip capture of EV isolated from serum after multi-step purification (see Figure 5) as well as directly from untreated serum. In complex samples such as untreated serum, the use of multivalent peptides showed to be particularly convenient to increase affinity and capturing specificity, in agreement with previous reports on the favourable role of multivalency in peptide microarrays [27].