Allergen-specific immunotherapy of Hymenoptera venom allergy – also a matter of diagnosis

Schiener, Maximilian; Graessel, Anke; Ollert, Markus; Schmidt‐Weber, Carsten B.; Blank, Simon

doi:10.1080/21645515.2017.1334745

Cited by 49 publications

(44 citation statements)

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“…The data we have obtained from these purified components, confirm the whole sequence data available in transcriptomic databases since 2015 [7], and this allows a thorough comparison with homologous components from other Hymenoptera. Moreover, the purified components will be used to demonstrate their relevance as allergens, by Component Resolved Diagnosis (CRD), in studies performed in platforms that can measure specific IgE in the sera of allergic patients ( [8,9]), which are useful to differentiate which can be the sensitizing species for each patient, as we also published in the past ( [10]), differentiating on Vespula versus. Polistes sensititization.…”

Section: Introductionmentioning

confidence: 99%

Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina)

2020

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The aim of this study was to purify potential allergenic components of Vespa velutina venom, the yellow legged Asian Hornet, and perform a preliminary characterization of the purified proteins. Starting from the whole venom of V.velutina, several chromatographic steps allowed to purify the phospholipase (named Vesp v 1), as well as the antigen 5 (Vesp v 5, the only allergenic component described as such so far). The two hyaluronidase isoforms found (Vesp v 2A and Vesp v 2B) cannot be separated from each other, but they are partially purified and characterized. Purity of the isolated proteins in shown by SDSPAGE, as well as by the results of the N-terminal sequencing. This characterization and nLC-MS/ MS data provide most of the sequence for Vesp v 1 and Vesp v 5 (72 and 84% coverage, respectively), confirming that the whole sequences of the isolated natural components match with the data available in public transcriptomic databases. It is of particular interest that Vesp v 1 is a glycosylated phospholipase, a fact that had only described so far for the corresponding allergen components of Dolichovespula maculata and Solenopsis invicta. The availability of the complete sequences of Vespa velutina components permits comparison with homologous sequences from other Hymenoptera. These data demonstrate the higher similarity among the species of the genera Vespa and Vespula, in comparison to Polistes species, as it is especially observed with the hyaluronidases isoforms: the isoform Vesp v 2A only exists in the former genera, and not in Polistes; in addition, the most abundant isoform (Vesp v 2B) exhibits 93% sequence identity with the Ves v 2 isoform of Vespula vulgaris. Finally, the isolated components might be useful for improving the diagnosis of patients that could be allergic to stings of this invasive Asian hornet, as it has been the case of an improved diagnosis and treatment of other Hymenoptera-sensitized patients.

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Section: Introductionmentioning

confidence: 99%

Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina)

2020

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“…Depending on the type of allergy and the physical condition of the patient, efficiency of allergen‐specific immunotherapy (AIT) varies strongly . Hence, there is a need for novel advanced strategies for the improvement of therapeutic efficacy of AIT in several disease conditions.…”

Section: Introductionmentioning

confidence: 99%

IL‐4 receptor α blockade prevents sensitization and alters acute and long‐lasting effects of allergen‐specific immunotherapy of murine allergic asthma

Rußkamp

Aguilar-Pimentel

Alessandrini

et al. 2019

Allergy

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Russkamp and Aguilar-Pimentel are contributed equally to this work as first authors.Abbreviations: AIT, allergen-specific immunotherapy; Alum, aluminum hydroxide magnesium hydroxide formulation; BAL, bronchoalveolar lavage; CHO, Chinese hamster ovary; FoxP3, forkhead box P3; GATA3, GATA-binding protein 3; HE, hematoxylin and eosin stain; IL-4M, IL-4 mutein, interleukin-4/interleukin-13 antagonist; i.n. AbstractBackground: Allergen-specific immunotherapy (AIT) is the only causal treatment for allergy. However, success rates vary depending on the type of allergy and disease background of the patient. Hence, strategies targeting an increased therapeutic efficacy are urgently needed. Here, the effects of blockade of IL-4 and IL-13 signaling on different phases of AIT were addressed. Methods:The impact of the recombinantly produced IL-4 and IL-13 antagonist IL-4 mutein (IL-4M) on allergic sensitization and AIT outcome in experimental allergic asthma were analyzed in a murine model. The effects of IL-4M administration were assessed prior/during sensitization, immediately after AIT under allergen challenge, and two weeks post-treatment. Results:Intervention with IL-4M prior/during sensitization led to strong induction of IgG1, IgG2a, IgG2b, and IgG3, decrease of specific and total IgE, as well as of IL-5 in serum. Similar effects on the serum immunoglobulin levels were observed immediately after IL4M-supplemented AIT during allergen challenge. Additionally, IL4M markedly suppressed type-2 cytokine secretion of splenocytes beyond the effect of AIT alone. These effects were equaled to those of AIT alone two weeks post-treatment. Intriguingly, here, IL-4M induced a sustained decrease of Th2-biased Tregs (ST2 + FOXP3 + GATA3 intermediate ).Conclusions: IL-4 and IL-13 blockade during experimental AIT demonstrates beneficial effects on immunological key parameters such as immunoglobulin and cytokine secretion immediately after AIT. Although two weeks later these effects were dropped to those of AIT alone, the number of potentially disease-triggering Th2-biased Tregs was further significantly decreased by IL-4M treatment. Hence, IL-4/IL13targeting therapies prime the immune memory in therapy success-favoring manner.

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“…The data we have obtained from these purified components, confirm the whole sequence data available in transcriptomic databases since 2015 [7], and this allows a thorough comparison with homologous components from other Hymenoptera. Moreover, the purified components will be used to demonstrate their relevance as allergens, by Component Resolved Diagnosis (CRD), in studies performed in platforms that can measure specific IgE in the sera of allergic patients ([8;9]), which are useful to differentiate which can be the sensitizing species for each patient, as we also published in the past ([10]), differentiating on Vespula vs. Polistes sensititization.…”

Section: Introductionmentioning

confidence: 99%

Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina)

Monsalve

Gutiérrez

Lombardero

2019

Preprint

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The aim of this study was to purify potential allergenic components of Vespa velutina venom, the yellow legged Asian Hornet, and perform a preliminary characterization of the purified proteins. Starting from the whole venom of V.velutina, several chromatographic steps allowed to purify the phospholipase (named Vesp v 1), as well as the antigen 5 (Vesp v 5, the only allergenic component described as such so far). The two hyaluronidase isoforms found (Vesp v 2A and Vesp v 2B) cannot be separated from each other, but they are partially purified and characterized. Purity of the isolated proteins in shown by SDSPAGE, as well as by the results of the N-terminal sequencing. This characterization and nLC-MS/MS data provide most of the sequence for Vesp v 1 and Vesp v 5 (72 and 84% coverage, respectively), confirming that the whole sequences of the isolated natural components match with the data available in public transcriptomic databases. It is of particular interest that Vesp v 1 is a glycosylated phospholipase, a fact that had only described so far for the corresponding allergen components of Dolichovespula maculata and Solenopsis invicta.The availability of the complete sequences of Vespa velutina components permits comparison with homologous sequences from other Hymenoptera. These data demonstrate the higher similarity among the species of the genera Vespa and Vespula, in comparison to Polistes species, as it is especially observed with the hyaluronidases isoforms: the isoform Vesp v 2A only exists in the former genera, and not in Polistes; in addition, the most abundant isoform (Vesp v 2B) exhibits 93% sequence identity with the Ves v 2 isoform of Vespula vulgaris.Finally, the isolated components might be useful for improving the diagnosis of patients that could be allergic to stings of this invasive Asian hornet, as it has been the case of an improved diagnosis and treatment of other Hymenoptera-sensitized patients.Data Availability StatementProteomic study data are deposited and made available publicly when data are published with the ProteomeExchange identifier PXD015381 in the Mass spectrometry Interactive Virtual Environment (MassIVE).Allergen nomenclature for Vesp v 5 (and also for any future demonstrated allergen from Vespa velutina) has been approved by the WHO/IUIS Committee (www.allergen.org); when this manuscript is accepted, the WHO/IUIS Committee will be informed so that the complete sequences included in this manuscript are also included in their database (with links to the UNIPROT database, who will also be informed that the data can be made public).

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Allergen-specific immunotherapy of Hymenoptera venom allergy – also a matter of diagnosis

Cited by 49 publications

References 149 publications

Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina)

Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina)

IL‐4 receptor α blockade prevents sensitization and alters acute and long‐lasting effects of allergen‐specific immunotherapy of murine allergic asthma

Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina)

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