Immunoglobulin E (IGE)-Binding FC Receptors

2016 ◽  
Author(s):  
Douglas M. Templeton ◽  
Michael Schwenk ◽  
Reinhild Klein ◽  
John H. Duffus
Keyword(s):  
Immunoglobulin E ◽  
Fc Receptors ◽  
Ige Binding

scholarly journals Lateral electromigration and diffusion of Fc epsilon receptors on rat basophilic leukemia cells: effects of IgE binding.

1984 ◽  
Vol 99 (3) ◽  
pp. 778-787 ◽  
Author(s):  
M A McCloskey ◽  
Z Y Liu ◽  
M M Poo
Keyword(s):  
Cell Surface ◽  
Immunoglobulin E ◽  
Fc Receptors ◽  
Lateral Diffusion ◽  
Surface Proteins ◽  
Ige Binding ◽  
The Difference ◽  
D Values ◽  
Rbl Cells ◽  
Basophilic Leukemia

We have used in situ electromigration and post-field relaxation (Poo, M.-m., 1981, Annu. Rev. Biophys. Bioeng., 10:245-276) to assess the effect of immunoglobulin E (IgE) binding on the lateral mobility of IgE-Fc receptors in the plasmalemma of rat basophilic leukemia (RBL) cells. Bound IgE sharply increased the receptor's electrokinetic mobility, whereas removal of cell surface neuraminic acids cut it to near zero. In contrast, we found only a small difference between the lateral diffusion coefficients (D) of vacant and IgE-occupied Fc receptors (D: 4 vs. 3 X 10(-10) cm2/s at 24 degrees C). This is true for monomeric rat IgE; with mouse IgE, the difference in apparent diffusion rates was slightly greater (D: 4.5 vs. 2.3 X 10(-10) cm2/s at 24 degrees C). This range of D values is close to that found in previous photobleaching studies of the IgE-Fc epsilon receptor complex in RBL cells and rat mast cells. Moreover, enzymatic depletion of cell coat components did not measurably alter the diffusion rate of IgE-occupied receptors. Thus, binding of fluorescent macromolecular probes to cell surface proteins need not severely impede lateral diffusion of the probed species. If the glycocalyx of RBL cells does limit lateral diffusion of the Fc epsilon receptor, it must act primarily on the receptor itself, rather than on receptor-bound IgE.

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.

scholarly journals Distinct Animal Food Allergens Form IgE-Binding Amyloids

Allergies ◽  
2020 ◽  
Vol 1 (1) ◽  
pp. 2
Author(s):  
Raquel Pérez-Tavarez ◽  
Milagros Castellanos ◽  
David Loli-Ausejo ◽  
María Pedrosa ◽  
José Luis Hurtado ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Allergic Patient ◽  
Full Length ◽  
Food Allergens ◽  
Native Structure ◽  
Animal Food ◽  
Ige Binding ◽  
D 12

Several animal food allergens assemble into amyloids under gastric-like environments. These aggregated structures provide Gad m 1 with an enhanced immunoglobulin E (IgE) interaction due to the fibrillation of the epitope regions. However, whether these properties are unique to Gad m 1 or shared by other food allergens has not yet been addressed. Using Bos d 5, Bos d 12 and Gal d 2 as allergen models and Gad m 1 as the control, aggregation reactions and the sera of milk, egg and fish allergic patients have been analyzed, assessing the IgE interactions of their amyloids. We found that amyloids formed by Bos d 12 and Gal d 2 full-length and truncated chains are recognized by the IgEs of milk and egg allergic patient sera. As with Gad m 1, in most cases amyloid recognition is higher than that of the native structure. Bos d 5 was not recognized under any fold by the IgE of the sera studied. These results suggest that the formation of IgE-binding amyloids could be a common feature to animal food allergens.

scholarly journals Lymphocytes with Immunoglobulin E Fc Receptors in Patients with Atopic Disorders

1979 ◽  
Vol 64 (3) ◽  
pp. 714-720 ◽  
Author(s):  
H. L. Spiegelberg ◽  
R. D. O'Connor ◽  
R. A. Simon ◽  
D. A. Mathison
Keyword(s):  
Immunoglobulin E ◽  
Fc Receptors

scholarly journals Conformational and Linear B-Cell Epitopes of Asp f 2, a Major Allergen of Aspergillus fumigatus, Bind Differently to Immunoglobulin E Antibody in the Sera of Allergic Bronchopulmonary Aspergillosis Patients

1999 ◽  
Vol 67 (5) ◽  
pp. 2284-2291 ◽  
Author(s):  
Banani Banerjee ◽  
Paul A. Greenberger ◽  
Jordan N. Fink ◽  
Viswanath P. Kurup
Keyword(s):  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
B Cell ◽  
Immunoglobulin E ◽  
Allergic Bronchopulmonary Aspergillosis ◽  
Amino Acid Sequences ◽  
Epitope Region ◽  
B Cell Epitopes ◽  
Ige Binding ◽  
Binding Regions

ABSTRACT Asp f 2 is a major Aspergillus fumigatus allergen involved in allergic bronchopulmonary aspergillosis. Knowledge of the B-cell epitopes may contribute to the understanding of immunoregulation and immunodiagnosis. To elucidate the immunoglobulin E (IgE) binding epitopes in the linear sequence of Asp f 2, we synthesized decamer peptides spanning the whole molecule of Asp f 2 on derivatized cellulose membranes and evaluated IgE binding in ABPA patient and control sera. Peptides three to five amino acids long were synthesized based on amino acid sequences within the IgE binding regions and evaluated for the specificity of epitope antibody interactions. Nine IgE binding regions were recognized in this protein of 268 amino acid residues. Of the nine epitopes, seven (ATQRRQI, RKYFG, HWR, YTTRR, DHFAD, ALEAYA, and THEGGQ) are present in the hydrophilic regions of Asp f 2. Immunologic evaluation of the three recombinant fragments, Asp f 2A encompassing the N-terminal epitope region, Asp f 2B without N- and C-terminal regions of the protein, and Asp f 2C representing C-terminal epitopes, revealed that either the N- or C-terminal region of the protein is essential for the correct folding and conformation for IgE antibody binding.

scholarly journals Ole e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE response in olive pollen allergic patients

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Pablo San Segundo-Acosta ◽  
Carmen Oeo-Santos ◽  
Ana Navas ◽  
Aurora Jurado ◽  
Mayte Villalba ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Pollen Allergy ◽  
Patient Specific ◽  
Specific Response ◽  
Surface Areas ◽  
Ige Reactivity ◽  
Ige Binding ◽  
Mediterranean Countries ◽  
Ige Response ◽  
Olive Pollen

Abstract Olive pollen is a major cause of immunoglobulin E (IgE)-mediated allergy in Mediterranean countries. It is expected to become a worldwide leading allergenic source because olive cultivation is increasing in many countries. Ole e 15 belongs to the cyclophilin pan-allergen family, which includes highly cross-reactive allergens from non-related plant, animal and mold species. Here, the amino acid differences between Ole e 15 and its weak cross-reactive human homolog PPIA were grafted onto Ole e 15 to assess the contribution of specific surface areas to the IgE-binding. Eight Ole e 15-PPIA chimeras were produced in E. coli, purified and tested with 20 sera from Ole e 15-sensitized patients with olive pollen allergy by ELISA experiments. The contribution of linear epitopes was analyzed using twelve overlapping peptides spanning the entire Ole e 15 sequence. All the patients displayed a diverse reduction of the IgE-reactivity to the chimeras, revealing a highly polyclonal and patient-specific response to Ole e 15. IgE-epitopes are distributed across the entire Ole e 15 surface. Two main surface areas containing relevant conformational epitopes have been characterized. This is the first study to identify important IgE-binding regions on the surface of an allergenic cyclophilin.

scholarly journals Analysis of Amino Acid Sequence Variations and Immunoglobulin E-Binding Epitopes of German Cockroach Tropomyosin

2004 ◽  
Vol 11 (5) ◽  
pp. 874-878 ◽  
Author(s):  
Kyoung Yong Jeong ◽  
Jongweon Lee ◽  
In-Yong Lee ◽  
Han-Il Ree ◽  
Chein-Soo Hong ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Single Molecule ◽  
Immunoglobulin E ◽  
German Cockroach ◽  
Amino Acid Sequences ◽  
Enzyme Linked Immunosorbent Assay ◽  
Rt Pcr ◽  
Ige Binding ◽  
Sequence Variations

ABSTRACT The allergenicities of tropomyosins from different organisms have been reported to vary. The cDNA encoding German cockroach tropomyosin (Bla g 7) was isolated, expressed, and characterized previously. In the present study, the amino acid sequence variations in German cockroach tropomyosin were analyzed in order to investigate its influence on allergenicity. We also undertook the identification of immunodominant peptides containing immunoglobulin E (IgE) epitopes which may facilitate the development of diagnostic and immunotherapeutic strategies based on the recombinant proteins. Two-dimensional gel electrophoresis and immunoblot analysis with mouse anti-recombinant German cockroach tropomyosin serum was performed to investigate the isoforms at the protein level. Reverse transcriptase PCR (RT-PCR) was applied to examine the sequence diversity. Eleven different variants of the deduced amino acid sequences were identified by RT-PCR. German cockroach tropomyosin has only minor sequence variations that did not seem to affect its allergenicity significantly. These results support the molecular basis underlying the cross-reactivities of arthropod tropomyosins. Recombinant fragments were also generated by PCR, and IgE-binding epitopes were assessed by enzyme-linked immunosorbent assay. Sera from seven patients revealed heterogeneous IgE-binding responses. This study demonstrates multiple IgE-binding epitope regions in a single molecule, suggesting that full-length tropomyosin should be used for the development of diagnostic and therapeutic reagents.

scholarly journals IgE Antibodies: From Structure to Function and Clinical Translation

Antibodies ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 19 ◽  
Author(s):  
Brian Sutton ◽  
Anna Davies ◽  
Heather Bax ◽  
Sophia Karagiannis
Keyword(s):  
Conformational Changes ◽  
Immunoglobulin E ◽  
Fc Receptors ◽  
Solid Tumours ◽  
Clinical Translation ◽  
Therapeutic Modality ◽  
Ige Antibodies ◽  
Effector Functions ◽  
Anti Cancer

Immunoglobulin E (IgE) antibodies are well known for their role in mediating allergic reactions, and their powerful effector functions activated through binding to Fc receptors FcεRI and FcεRII/CD23. Structural studies of IgE-Fc alone, and when bound to these receptors, surprisingly revealed not only an acutely bent Fc conformation, but also subtle allosteric communication between the two distant receptor-binding sites. The ability of IgE-Fc to undergo more extreme conformational changes emerged from structures of complexes with anti-IgE antibodies, including omalizumab, in clinical use for allergic disease; flexibility is clearly critical for IgE function, but may also be exploited by allosteric interference to inhibit IgE activity for therapeutic benefit. In contrast, the power of IgE may be harnessed to target cancer. Efforts to improve the effector functions of therapeutic antibodies for cancer have almost exclusively focussed on IgG1 and IgG4 subclasses, but IgE offers an extremely high affinity for FcεRI receptors on immune effector cells known to infiltrate solid tumours. Furthermore, while tumour-resident inhibitory Fc receptors can modulate the effector functions of IgG antibodies, no inhibitory IgE Fc receptors are known to exist. The development of tumour antigen-specific IgE antibodies may therefore provide an improved immune functional profile and enhanced anti-cancer efficacy. We describe proof-of-concept studies of IgE immunotherapies against solid tumours, including a range of in vitro and in vivo evaluations of efficacy and mechanisms of action, as well as ex vivo and in vivo safety studies. The first anti-cancer IgE antibody, MOv18, the clinical translation of which we discuss herein, has now reached clinical testing, offering great potential to direct this novel therapeutic modality against many other tumour-specific antigens. This review highlights how our understanding of IgE structure and function underpins these exciting clinical developments.

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