Changes in the Antigenic and Immunoglobulin E–Binding Properties of Hen's Egg Albumin with the Combination of Heat and Gamma Irradiation Treatment

2002 ◽  
Vol 65 (7) ◽  
pp. 1192-1195 ◽  
Author(s):  
MI-JUNG KIM ◽  
JU-WOON LEE ◽  
HONG-SUN YOOK ◽  
SOO-YOUNG LEE ◽  
MYUNG-CHUL KIM ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Gamma Irradiation ◽  
Immunoglobulin E ◽  
Binding Properties ◽  
Egg Albumin ◽  
Ige Binding ◽  
Irradiation Treatment ◽  
Hen’S Egg ◽  
Antigenic Properties ◽  
Irradiation Sample

This study was carried out to evaluate the changes in the allergenic and antigenic properties of hen's egg albumin (ovalbumin [OVA]) with the combination of heat and gamma irradiation treatment. OVA solution samples were treated by (i) heating (sample 1), (ii) irradiation after heating (sample 2), and (iii) heating after irradiation (sample 3). Samples were isothermally heated and irradiated at the absorption dose of 10 kGy. Competitive indirect enzyme-linked immunosorbent assays (ELISAs) were performed with blood serum to test the ability of treated OVA to bind to immunoglobulin E (IgE) and mouse murine monoclonal antibody (IgG). OVA's ability to bind to mouse IgG changed upon heating at 75°C, and its ability to bind to egg-allergic IgE changed upon heating at 80°C. The ELISAs showed that egg-allergic IgE did not recognize OVA very well when heated at ≥80°C, while mouse IgG retained better activity under these conditions. Egg-allergic IgE binding was low both for OVA samples treated by heating and for samples treated by irradiation followed by heating. These results show that allergies induced by OVA could be effectively reduced by the combination of heat and gamma irradiation treatment.

scholarly journals Single Chain Variable Fragment Fused to Maltose Binding Protein: A Modular Nanocarrier Platform for the Targeted Delivery of Antitumorals

2021 ◽  
Author(s):  
Francisco J. Reche-Perez ◽  
Simona Plesselova ◽  
Eduardo De los Reyes-Berbel ◽  
Mariano Ortega-Muñoz ◽  
F. Javier Lopez-Jaramillo ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Targeted Delivery ◽  
Specific Binding ◽  
Protein A ◽  
Antibody Fragments ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Binding Properties ◽  
Single Chain Variable Fragments ◽  
Selective Delivery

The use of the specific binding properties of monoclonal antibody fragments such as single-chain variable fragments (ScFv) for the selective delivery of antitumor therapeutics for cancer cells is attractive due...

Partial Amino Acid Sequence of a Cellulase-Like Component with IgE-Binding Properties from Stachybotrys chartarum

2004 ◽  
Vol 133 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Marja Kärkkäinen ◽  
Päivi Raunio ◽  
Jaakko Rautiainen ◽  
Seppo Auriola ◽  
Kaj Hinke ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Stachybotrys Chartarum ◽  
Partial Amino Acid Sequence ◽  
Binding Properties ◽  
Ige Binding

scholarly journals Functional study of a monoclonal antibody to IgE Fc receptor (Fc epsilon R2) of eosinophils, platelets, and macrophages.

1986 ◽  
Vol 164 (1) ◽  
pp. 72-89 ◽  
Author(s):  
M Capron ◽  
T Jouault ◽  
L Prin ◽  
M Joseph ◽  
J C Ameisen ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
B Lymphocyte ◽  
Specific Binding ◽  
Polyclonal Antibodies ◽  
Fc Receptor ◽  
The Other ◽  
Functional Study ◽  
Low Density ◽  
Fluorescence Staining ◽  
Ige Binding

An IgM mAb (BB10) was produced by immunization of mice with human eosinophils purified according to their abnormal low density ("hypodense" cells), and previously shown to exhibit increased IgE-dependent antiparasite cytotoxicity. This BB10 antibody, selected for positive fluorescence staining of hypodense blood or lung eosinophils and low or negative staining of normodense eosinophils or neutrophils, could strongly inhibit IgE-dependent cytotoxicity of human eosinophils and platelets. The specificity for the IgE Fc receptor was suggested by the high levels of inhibition of IgE rosettes formed by eosinophils after incubation with the purified IgM fraction of BB10, whereas other receptors (Fc gamma R, CR1) were not affected. On the other hand, BB10, able to inhibit rat eosinophil Fc epsilon R, did not react with the IgE Fc receptor on mast cells or basophils. A technique using radioiodinated BB10 allowed us to quantify the specific binding of BB10 to human eosinophils and platelets. Competition experiments revealed a crossinhibition between the binding of BB10 and IgE, suggesting the specificity of BB10 for the IgE binding site of eosinophil, platelet, and monocyte Fc epsilon R. Three proteins having extrapolated Mr of 32,000, 43,000-45,000, and 97,000 were found in the platelet extract eluted from a BB10 or from an IgE immunosorbent column. These findings confirm the similarities between IgE Fc receptors on human eosinophils, platelets, and macrophages, already observed with polyclonal antibodies directed against the B lymphocyte Fc epsilon receptor. They suggest, moreover, that the mAb BB10 can represent a good reagent for further investigations on the structure and the functions of this IgE Fc receptor (Fc epsilon R2).

Preclinical Safety and Pharmacology of an Anti-Human Interleukin-13 Monoclonal Antibody in Normal Macaques and in Macaques with Allergic Asthma

2008 ◽  
Vol 27 (5) ◽  
pp. 351-358 ◽  
Author(s):  
Pauline L. Martin ◽  
Dusti Fisher ◽  
William Glass ◽  
Karyn O’Neil ◽  
Anuk Das ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Allergic Asthma ◽  
Immunoglobulin E ◽  
Cynomolgus Macaque ◽  
Lavage Fluid ◽  
Antigen Challenge ◽  
Interleukin 13 ◽  
Lung Eosinophilia

Interleukin-13 (IL-13) plays a central role in chronic airway diseases, including asthma. These studies were conducted to evaluate the safety of administration of a human anti-IL-13 monoclonal antibody (mAb) to normal macaques and in macaques with allergic asthma. In addition, serum and bronchioalveolar lavage fluid were collected from allergic cynomolgus macaques in order to identify potential surrogate markers of IL-13 pharmacology that could be useful for subsequent clinical trials. In vitro studies demonstrated that the anti-IL-13 mAb inhibited the pharmacological actions of both human and cynomolgus macaque IL-13. Allergic macaques were treated systemically with 10 mg/kg anti-IL-13 mAb 1 day prior to inhaled Ascaris suum antigen challenge. Normal macaques were dosed intravenously with anti-IL-13 once per week for 3 weeks at doses of 10 or 50 mg/kg. Treatment of macaques with the anti-IL-13 mAb was not associated with any toxicologically significant findings. A slight treatment-related but nonadverse decrease in platelet counts was observed in both the normal and allergic macaques. In allergic macaques, the anti-IL-13 mAb treatment did not affect lung function, lung eosinophilia, or serum or BAL immunoglobulin E (IgE) concentrations but did produce a reduction in BAL and serum eotaxin concentrations ( p < .05) at 6 h post antigen challenge. This study shows that administration of an anti-IL-13 mAb was well tolerated in both normal and allergic asthmatic macaques and that serum eotaxin concentrations may be a useful early in vivo marker for evaluating IL-13 inhibition in patients with asthma.

scholarly journals Detection and identification of allergens from Canadian mustard varieties of Sinapis alba and Brassica juncea

Biomolecules ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 489 ◽  
Author(s):  
L’Hocine ◽  
Pitre ◽  
Achouri
Keyword(s):  
Brassica Juncea ◽  
Protein Extraction ◽  
Immunoglobulin E ◽  
Sinapis Alba ◽  
Cross Reactivity ◽  
Protein Profiling ◽  
Ige Reactivity ◽  
Ige Binding ◽  
Reducing Conditions ◽  
Detection And Identification

Currently, information on the allergens profiles of different mustard varieties is rather scarce. Therefore, the objective of this study was to assess protein profiles and immunoglobulin E (IgE)-binding patterns of selected Canadian mustard varieties. Optimization of a non-denaturing protein extraction from the seeds of selected mustard varieties was first undertaken, and the various extracts were quantitatively and qualitatively analyzed by means of protein recovery determination and protein profiling. The IgE-binding patterns of selected mustard seeds extracts were assessed by immunoblotting using sera from mustard sensitized and allergic individuals. In addition to the known mustard allergens—Sin a 2 (11S globulins), Sin a 1, and Bra j 1 (2S albumins)—the presence of other new IgE-binding protein bands was revealed from both Sinapis alba and Brassica juncea varieties. Mass spectrometry (MS) analysis of the in-gel digested IgE-reactive bands identified the unknown ones as being oleosin, β-glucosidase, enolase, and glutathione-S transferase proteins. A bioinformatic comparison of the amino acid sequence of the new IgE-binding mustard proteins with those of know allergens revealed a number of strong homologies that are highly relevant for potential allergic cross-reactivity. Moreover, it was found that Sin a 1, Bra j 1, and cruciferin polypeptides exhibited a stronger IgE reactivity under non-reducing conditions in comparison to reducing conditions, demonstrating the recognition of conformational epitopes. These results further support the utilization of non-denaturing extraction and analysis conditions, as denaturing conditions may lead to failure in the detection of important immunoreactive epitopes.

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