Human IgE is efficiently produced in glycosylated and biologically active form in lepidopteran cells

Bantleon, Frank; Wolf, Sara; Seismann, Henning; Dam, Svend; Lorentzen, Andrea; Miehe, Michaela; Jabs, Frederic; Jakob, Thilo; Plum, Melanie; Spillner, Edzard

doi:10.1016/j.molimm.2016.02.013

Cited by 9 publications

(10 citation statements)

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“…In keeping with the molecular similarity between helminth oligosaccharides and classical CCD, IgE antibodies reacting with both groups do occur. However, a study with a monoclonal CCD‐specific IgE Ab showed limited cross‐reactivity between classical CCDs and helminth extract in ImmunoCAP, suggesting possible differences in recognizing oligosaccharides of these two groups 83 …”

Section: Group D Oligosaccharide Epitopes That Are the Targets For Ige Ab Responses To Schistosomes And Other Helminthsmentioning

confidence: 99%

“…However, a study with a monoclonal CCD-specific IgE Ab showed limited cross-reactivity between classical CCDs and helminth extract in ImmunoCAP, suggesting possible differences in recognizing oligosaccharides of these two groups. 83 Although the presence of oligosaccharides on other helminths is well established, there is relatively little evidence regarding the significance of IgE antibodies to these epitopes. A recent study provides evidence that IgE to classical CCD, particularly those with an alpha-1, 3-fucose epitope, may not just be an epiphenomenon of parasite exposure but may be implicated in the protective effect of certain environmental and geohelminth exposures against asthma.…”

Section: G Roup D Oli G Osaccharide Epitope S That Are the Targ E Ts For Ige Ab Re S P On S E S To Schis Tosome S And Other Helminth Smentioning

confidence: 99%

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Carbohydrate epitopes currently recognized as targets for IgE antibodies

Platts‐Mills

Hilger

Jappe

et al. 2021

Allergy

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Until recently, glycan epitopes have not been documented by the WHO/IUIS Allergen Nomenclature Sub-Committee. This was in part due to scarce or incomplete information on these oligosaccharides, but also due to the widely held opinion that IgE to these epitopes had little or no relevance to allergic symptoms. Most IgE-binding glycans recognized up to 2008 were considered to be "classical" cross-reactive carbohydrate determinants (CCD) that occur in insects, some helminths and throughout the plant kingdom. Since 2008, the prevailing opinion on lack of clinical relevance of IgEbinding glycans has been subject to a reevaluation. This was because IgE specific for the mammalian disaccharide galactose-alpha-1,3-galactose (alpha-gal) was identified as a cause of delayed anaphylaxis to mammalian meat in the United States, an observation that has been confirmed by allergists in many parts of the world. Several experimental studies have shown that oligosaccharides with one or more terminal alpha-gal How to cite this article: Platts-Mills TA, Hilger C, Jappe U, et al. Carbohydrate epitopes currently recognized as targets for IgE

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Section: Group D Oligosaccharide Epitopes That Are the Targets For Ige Ab Responses To Schistosomes And Other Helminthsmentioning

confidence: 99%

Section: G Roup D Oli G Osaccharide Epitope S That Are the Targ E Ts For Ige Ab Re S P On S E S To Schis Tosome S And Other Helminth Smentioning

confidence: 99%

Carbohydrate epitopes currently recognized as targets for IgE antibodies

Platts‐Mills

Hilger

Jappe

et al. 2021

Allergy

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“…Proteins were expressed in HEK293 or insect cells and purified to homogeneity. 19 For EM grid preparation, IgE and IgE-ligelizumab…”

Section: Me Thodsmentioning

confidence: 99%

Structure of intact IgE and the mechanism of ligelizumab revealed by electron microscopy

Jensen

Jabs

Miehe

et al. 2020

Allergy

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Background: IgE is the central antibody isotype in TH2-biased immunity and allergic diseases. The structure of intact IgE and the impact of IgE-targeting molecules on IgE however remain elusive. In order to obtain insights into IgE biology and the clinical impact, we aimed for structure determination of IgE and the complex of IgE with the anti-IgE antibody ligelizumab. Methods: Structures of two distinct intact IgE with specificity for cross-reactive carbohydrate determinants and Der p 2 as well as complexes of ligelizumab-Fab with IgE and IgE Fc were assessed by negative stain electron microscopy and solution scattering. Inhibition of IgE binding and displacement of receptor-bound IgE were assessed using cellular assays, basophil activation testing and ELIFAB assays. Results: Our data reveal that the investigated IgE molecules share an overall rigid conformation. In contrast to the IgE Fc fragment, the IgE Fc in intact IgE is significantly less asymmetrically bent. The proximal and the distal Fabs are rigidly tethered to the Fc. Binding of ligelizumab to IgE in a 2:1 stoichiometry induces an extended and twofold symmetrical conformation of IgE, which retains a rigid Fab-Fc architecture. Analyses of effector cell activation revealed that ligelizumab inhibits IgE binding without displacing receptor-bound IgE. Together with an interference of CD23 binding, the data underline a functional activity similar to omalizumab. Conclusions: Our data reveal the first structures of intact IgE suggesting that the IgE Fab is fixed relative to the Fc. Furthermore, we provide a structural rationale for the inhibitory mechanism of ligelizumab.

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“…AllergoOncology, the emerging discipline of cancer immunology aiming to exploit features of allergy-related immunity to treat tumors,1, 2, 3 has catalyzed the development of tumor-specific IgE mAbs as powerful alternatives to commonly used therapeutic IgGs 4, 5, 6. IgE, which is associated typically with the pathogenesis of allergic responses and is known for Fc-mediated protective effects in parasitic infection clearance, presents exciting opportunities to unleash previously untapped immune mechanisms and effective antitumor surveillance when focused against cancer antigens.…”

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confidence: 99%