Abstract

Purpose of ReviewIn Hymenoptera venom allergy, the research focus has moved from whole venoms to individual allergenic molecules. Api m 10 (icarapin) has been described as a major allergen of honeybee venom (HBV) with potentially high relevance for diagnostics and therapy of venom allergy. Here, we review recent studies on Api m 10 characteristics as well as its role in component-resolved diagnostics and potential implications for venom-specific immunotherapy (VIT).Recent FindingsApi m 10 is a major allergen of low abundance in HBV. It is an obviously unstable protein of unknown function that exhibits homologs in other insect species. Despite its low abundance in HBV, 35 to 72% of HBV-allergic patients show relevant sensitization to this allergen. Api m 10 is a marker allergen for HBV sensitization, which in many cases can help to identify primary sensitization to HBV and, hence, to discriminate between genuine sensitization and cross-reactivity. Moreover, Api m 10 might support personalized risk stratification in VIT, as dominant sensitization to Api m 10 has been identified as risk factor for treatment failure. This might be of particular importance since Api m 10 is strongly underrepresented in some therapeutic preparations commonly used for VIT.SummaryAlthough the role of Api m 10 in HBV allergy and tolerance induction during VIT is not fully understood, it certainly is a useful tool to unravel primary sensitization and individual sensitization profiles in component-resolved diagnostics (CRD). Moreover, a potential of Api m 10 to contribute to personalized treatment strategies in HBV allergy is emerging.

Highlights

  • Allergic reactions to stings of honeybees may represent severe and even fatal scenarios

  • Hymenoptera venom allergy can be effectively cured by venom-specific immunotherapy (VIT), provided that the culprit insect can be correctly identified

  • These analyses demonstrated that venom proteins of high abundance, such as the well-characterized phospholipase A2 (Api m 1), and proteins that make up only minute amounts of the venom, may represent major specific IgE (sIgE)-sensitizing components

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Summary

Introduction

Allergic reactions to stings of honeybees may represent severe and even fatal scenarios. VIT with honeybee venom (HBV) is reported to be effective in 77 to 84% of HBV-allergic patients and, is less effective as VIT with vespid venom (91–96%) [1]. Reasons for this discrepancy are so far not clear and a matter of debate. A honeybee sting contains approximately 59 (± 7) μg of proteins/peptides [2], which are the main triggers of allergic reactions to the venom. In the last two decades, the evolvement of genomic and proteomic approaches has led to the identification of a variety of formerly unknown HBV proteins [3, 4] and shifted the view from the whole venom to individual allergenic molecules [5]. Detailed component-resolved analyses of specific IgE (sIgE) sensitization of HBV-allergic patients using

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