scholarly journals Characterization of New Allergens from the Venom of the European Paper Wasp Polistes dominula

Toxins ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 559
Author(s):  
Johannes Grosch ◽  
Bernadette Eberlein ◽  
Sebastian Waldherr ◽  
Mariona Pascal ◽  
Clara San Bartolomé ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Cross Reactivity ◽  
Paper Wasp ◽  
Hymenoptera Venom ◽  
Venom Allergy ◽  
Allergen Specific Immunotherapy ◽  
Polistes Dominula ◽  
Factor C ◽  
Venom Proteins

Discriminating Polistes dominula and Vespula spp. venom allergy is of growing importance worldwide, as systemic reactions to either species’ sting can lead to severe outcomes. Administering the correct allergen-specific immunotherapy is therefore a prerequisite to ensure the safety and health of venom-allergic patients. Component-resolved diagnostics of Hymenoptera venom allergy might be improved by adding additional allergens to the diagnostic allergen panel. Therefore, three potential new allergens from P. dominula venom—immune responsive protein 30 (IRP30), vascular endothelial growth factor C (VEGF C) and phospholipase A2 (PLA2)—were cloned, recombinantly produced and biochemically characterized. Sera sIgE titers of Hymenoptera venom-allergic patients were measured in vitro to assess the allergenicity and potential cross-reactivity of the venom proteins. IRP30 and VEGF C were classified as minor allergens, as sensitization rates lay around 20–40%. About 50% of P. dominula venom-allergic patients had measurable sIgE titers directed against PLA2 from P. dominula venom. Interestingly, PLA2 was unable to activate basophils of allergic patients, questioning its role in the context of clinically relevant sensitization. Although the obtained results hint to a questionable benefit of the characterized P. dominula venom proteins for improved diagnosis of venom-allergic patients, they can contribute to a deeper understanding of the molecular mechanisms of Hymenoptera venoms and to the identification of factors that determine the allergenic potential of proteins.

scholarly journals Steroidal Androgens and Nonsteroidal, Tissue-Selective Androgen Receptor Modulator, S-22, Regulate Androgen Receptor Function through Distinct Genomic and Nongenomic Signaling Pathways

2008 ◽  
Vol 22 (11) ◽  
pp. 2448-2465 ◽  
Author(s):  
Ramesh Narayanan ◽  
Christopher C. Coss ◽  
Muralimohan Yepuru ◽  
Jeffrey D. Kearbey ◽  
Duane D. Miller ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Intracellular Signaling ◽  
Molecular Mechanisms ◽  
Levator Ani ◽  
Reproductive Organs ◽  
Cross Reactivity ◽  
Levator Ani Muscle ◽  
Xenopus Laevis Oocyte ◽  
Muscle Weight

Abstract Androgen receptor (AR) ligands are important for the development and function of several tissues and organs. However, the poor oral bioavailability, pharmacokinetic properties, and receptor cross-reactivity of testosterone, coupled with side effects, place limits on its clinical use. Selective AR modulators (SARMs) elicit anabolic effects in muscle and bone, sparing reproductive organs like the prostate. However, molecular mechanisms underlying the tissue selectivity remain ambiguous. We performed a variety of in vitro studies to compare and define the molecular mechanisms of an aryl propionamide SARM, S-22, as compared with dihydrotestosterone (DHT). Studies indicated that S-22 increased levator ani muscle weight but decreased the size of prostate in rats. Analysis of the upstream intracellular signaling events indicated that S-22 and DHT mediated their actions through distinct pathways. Modulation of these pathways altered the recruitment of AR and its cofactors to the PSA enhancer in a ligand-dependent fashion. In addition, S-22 induced Xenopus laevis oocyte maturation and rapid phosphorylation of several kinases, through pathways distinct from steroids. These studies reveal novel differences in the molecular mechanisms by which S-22, a nonsteroidal SARM, and DHT mediate their pharmacological effects.

scholarly journals Shedding Light on the Venom Proteomes of the Allergy-Relevant Hymenoptera Polistes dominula (European Paper Wasp) and Vespula spp. (Yellow Jacket)

Toxins ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 323 ◽  
Author(s):  
Johannes Grosch ◽  
Christiane Hilger ◽  
Maria Beatrice Bilò ◽  
Stephanie Kler ◽  
Maximilian Schiener ◽  
...  
Keyword(s):  
Specific Immunotherapy ◽  
Biochemical Properties ◽  
Paper Wasp ◽  
Allergic Reactions ◽  
Liquid Chromatography Mass Spectrometry ◽  
Venom Allergy ◽  
Closely Related Species ◽  
Yellow Jacket ◽  
Polistes Dominula ◽  
Marker Allergens

Allergic reactions to stings of Hymenoptera species can have serious or even fatal consequences. If the identification of the culprit insect is possible, venom-specific immunotherapy effectively cures Hymenoptera venom allergies. Although component-resolved diagnostics has strongly evolved in recent years, the differentiation between allergies to closely related species such as Polistes dominula and Vespula spp. is still challenging. In order to generate the basis for new diagnostic and therapeutic strategies, this study aims at resolving the venom proteomes (venomes) of these species. The venoms of P. dominula and Vespula spp. (V. germanica, V. vulgaris) were analyzed by liquid chromatography-mass spectrometry. Resulting proteins were characterized regarding their function, localization and biochemical properties. The analyses yielded 157 proteins in Vespula spp. and 100 in P. dominula venom; 48 proteins, including annotated allergens, were found in both samples. In addition to a variety of venom trace molecules, new allergen candidates such as icarapin-like protein and phospholipase A2 were identified. This study elucidates the venomes of closely related allergy-eliciting Hymenoptera species. The data indicates that relying on marker allergens to differentiate between P. dominula and Vespula spp. venom allergy is probably insufficient and that strategies using cross-reactive major allergens could be more promising.

In vitro hymenoptera venom allergy diagnosis: improved by screening for cross-reactive carbohydrate determinants and reciprocal inhibition

Allergy ◽  
2006 ◽  
Vol 61 (10) ◽  
pp. 1220-1229 ◽  
Author(s):  
U. Jappe ◽  
M. Raulf-Heimsoth ◽  
M. Hoffmann ◽  
G. Burow ◽  
C. Hubsch-Muller ◽  
...  
Keyword(s):  
Reciprocal Inhibition ◽  
Hymenoptera Venom ◽  
Allergy Diagnosis ◽  
Venom Allergy ◽  
Hymenoptera Venom Allergy

Dissecting cross-reactivity in hymenoptera venom allergy by circumvention of α-1,3-core fucosylation

2010 ◽  
Vol 47 (4) ◽  
pp. 799-808 ◽  
Author(s):  
Henning Seismann ◽  
Simon Blank ◽  
Ingke Braren ◽  
Kerstin Greunke ◽  
Liliana Cifuentes ◽  
...  
Keyword(s):  
Cross Reactivity ◽  
Hymenoptera Venom ◽  
Venom Allergy ◽  
Hymenoptera Venom Allergy ◽  
Core Fucosylation

The use of cellular in vitro assays in the diagnosis of hymenoptera venom allergy

2005 ◽  
Vol 115 (2) ◽  
pp. S108 ◽  
Author(s):  
K. Scherer ◽  
J.M. Weber ◽  
T.M. Jermann ◽  
A. Krautheim ◽  
D. Keefe ◽  
...  
Keyword(s):  
In Vitro Assays ◽  
Hymenoptera Venom ◽  
Venom Allergy ◽  
Hymenoptera Venom Allergy

scholarly journals Cellular in vitro Assays in the Diagnosis of Hymenoptera Venom Allergy

2008 ◽  
Vol 146 (2) ◽  
pp. 122-132 ◽  
Author(s):  
K. Scherer ◽  
J.M. Weber ◽  
T.M. Jermann ◽  
A. Krautheim ◽  
E. Tas ◽  
...  
Keyword(s):  
In Vitro Assays ◽  
Hymenoptera Venom ◽  
Venom Allergy ◽  
Hymenoptera Venom Allergy

FcεRI Cluster Size Determines Effective Mast Cell Desensitization without Effector Responses in vitro

2021 ◽  
pp. 1-9
Author(s):  
Yuka Nagata ◽  
Ryo Suzuki
Keyword(s):  
Mast Cell ◽  
Molecular Mechanisms ◽  
Cluster Formation ◽  
Tolerance Induction ◽  
Specific Ige ◽  
Cell Surface Expression ◽  
Optimal Size ◽  
Allergen Specific Immunotherapy ◽  
The Impact

<b><i>Background:</i></b> Allergen-specific desensitization of mast cell (MC) IgE receptors (FcεRI) is an important mechanism of allergen-specific immunotherapy that enables tolerance induction via systemic desensitization. Experimental in vitro IgE-mediated MC desensitization is a potential tool to understand the molecular mechanisms underlying this therapy. Desensitized MCs exhibit internalized IgE and its FcεRI receptors in response to suboptimal doses of allergen without provoking activation. The ovalbumin (OVA) allergen exhibits altered allergenicity upon heat treatment. MC reactions are fundamentally regulated by allergen features (i.e., allergenicity); however, the effects of allergenicity on desensitization remain unclear. <b><i>Objectives:</i></b> This study aimed to examine the impact of allergenicity on the establishment of in vitro MC desensitization using naive OVA (nOVA) and heated OVA (hOVA), which could induce varying MC effector responses. <b><i>Method:</i></b> Bone marrow-derived MCs (BMMCs) were sensitized with OVA-specific IgE, desensitized with sequentially increasing doses of nOVA or hOVA at 10-min intervals, and challenged with nOVA. To evaluate desensitization, the cell surface expression level and subcellular localization of FcεRI-bound IgE were analyzed before and after the final nOVA challenge. MC activation was determined by measuring the release of β-hexosaminidase into supernatants. <b><i>Results:</i></b> Desensitized cells exhibited impaired activation following OVA challenge. Both nOVA and hOVA induced BMMC desensitization under different conditions. Formation of small IgE-FcεRI cluster BMMCs, which adequately represent the desensitized state, was significant. The size of the internalized IgE-FcεRI clusters might be correlated with the desensitized state of MCs. <b><i>Conclusions:</i></b> We demonstrate that the optimal size of IgE-FcεRI clusters for in vitro BMMC desensitization differed significantly depending on allergenicity, and the efficacy of desensitization was reflected by IgE-FcεRI cluster formation. Our study provides information on the characteristics of IgE-FcεRI internalization for successful desensitization in vitro.

Stinging Insect Allergens

2020 ◽  
Vol 21 (2) ◽  
pp. 142-152 ◽  
Author(s):  
Le Cui ◽  
Ying-Yang Xu ◽  
Xiu-Jie Wang ◽  
Kai Guan
Keyword(s):  
Specific Ige ◽  
Cross Reactivity ◽  
Hymenoptera Venom ◽  
Venom Allergy ◽  
Hymenoptera Venom Allergy ◽  
Predictive Values ◽  
Common Causes ◽  
History Of ◽  
The Common ◽  
Stinging Insect

Hymenoptera venom allergy is one of the common causes of anaphylaxis. However, when physicians make the diagnosis of Hymenoptera venom allergy, the history of being stung is not always consistent with the results of venom-specific IgE. With the development of component-resolved diagnosis, it is possible to accurately localize an allergic reaction to certain sensitized proteins. This paper reviewed the studies that have addressed the identified allergenicity and cross-reactivity of Hymenoptera venom allergens accepted by the WHO/IUIS Nomenclature Sub-committee, the componentresolved diagnosis of Hymenoptera venom allergy and its predictive values for the efficacy and safety of venom immunotherapy. Also special attention was paid to the spread of Hymenoptera venom allergy in Asian countries.

scholarly journals Marker allergens in Hymenoptera venom allergy — Characteristics and potential use in precision medicine

2020 ◽  
Author(s):  
Simon Blank ◽  
Maria Beatrice Bilò ◽  
Johannes Grosch ◽  
Carsten B. Schmidt-Weber ◽  
Markus Ollert ◽  
...  
Keyword(s):  
Clinical History ◽  
Cross Reactivity ◽  
Positive Test ◽  
Test Results ◽  
Hymenoptera Venom ◽  
Venom Allergy ◽  
Therapeutic Decisions ◽  
Threatening Condition ◽  
Primary Sensitization ◽  
Marker Allergens

Abstract Background A comprehensive diagnostic work-up is essential to ensure adequate patient management for the potentially life-threatening condition of Hymenoptera venom allergy (HVA). This includes an unambiguous identification of the allergy-relevant venom as prerequisite for successful venom-specific immunotherapy (VIT). If the clinical history does not allow the identification of the culprit insect, diagnosis is often hampered by positive test results to various venoms. Modern component-resolved diagnostics (CRD) applying marker allergens of Hymenoptera venoms has created new opportunities which facilitate therapeutic decisions and may allow personalized risk stratification for individual patients. Methods Comprehensive literature search and critical analysis of recently published studies on Hymenoptera venom allergens and CRD. Results and discussion Changing the research focus from whole venom extracts to individual allergenic molecules led to the development of CRD in HVA. The currently available CRD is a valuable tool to resolve cross-reactivity and primary sensitization, particularly in honeybee and vespid venom allergy. Hence, CRD has simplified therapeutic decisions in case of multiple positive test results, especially in patients who were not able to identify the culprit insect or in cases of discrepancies between clinical history and classical diagnostic results. Moreover, there is first evidence that sensitization to particular allergens might serve as biomarkers to predict risk for severe side-effects during VIT or even for VIT failure. To date, a clear limitation of CRD is the currently available allergen panel which does not allow a definite resolution of allergy to different vespid species such as yellow jackets and European paper wasps.

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