Antigen 5 Allergens of Hymenoptera Venoms and Their Role in Diagnosis and Therapy of Venom Allergy

Abstract

Purpose of Review Stings of Hymenoptera of the superfamily Vespoidea such as yellow jackets, paper wasps or stinging ants are common triggers for severe and even fatal allergic reactions. Antigen 5 allergens are potent allergens in the majority of these venoms with major importance for diagnosis and therapy. Reviewed here are the characteristics of antigen 5 allergens, their role in component-resolved diagnostics as well as current limitations of the available diagnostics for proper therapeutic decisions. Recent Findings Antigens 5 are proteins of unknown function in Hymenoptera venoms with high allergenic potency. They represent key elements in component-resolved diagnosis to discriminate between honeybee and vespid venom allergy. However, due to their pronounced cross-reactivity, there are remaining diagnostic and therapeutic challenges that have to be addressed. Summary Antigens 5 are highly relevant venom allergens of the Vespoidea superfamily. Although their use in componentresolved diagnosis facilitates dissection of cross-reactivity and primary allergy in double sensitization to honeybee and vespid venom, new diagnostic concepts are needed to discriminate between allergies to different vespid species.

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

“…Antigen 5 (Ag5) proteins are listed as important major venom allergens for most allergy-relevant Vespoidea species [34,56]. Although Ag5 allergens are one of the most abundant proteins in most Vespoidea venoms, their function within the venoms remains largely unclear.…”

“…Sensitization to the second commercially available Ag5, Pol d 5 from PDV, in primary PDV-sensitized patients is difficult to assess since a substantial percentage of the respective patient populations is DS to PDV and YJV with unknown primary sensitizer. Nevertheless, the available studies suggest that Ag5 proteins represent the most potent allergens in almost all studies allergy-eliciting Vespoidea species [56].…”

Proteo-Trancriptomic Analyses Reveal a Large Expansion of Metalloprotease-Like Proteins in Atypical Venom Vesicles of the Wasp Meteorus pulchricornis (Braconidae)

“…PR-1 proteins are ubiquitous in plant species and it is suggested that PR-1 has a broad antimicrobial function. Antigens 5 are proteins of unknown function in Hymenoptera venoms with strong allergenic potency [ 85 ]. When we aligned the first CAP domain of contig 2455 with the Hymenoptera antigen 5 sequences (which have only one domain), we obtained a good match with about 35–40% identity ( Figure 9 ).…”

“… Alignment of the first CAP domain of contig 2455 (Mp-CRISP) with selected sequences of hymenoptera antigen 5 allergens. The CAP signature motifs are shaded in grey and conserved residues that form the putative active site are shaded in cyan [ 85 ]. Cysteine residues that form disulphide bridges in Ag5 proteins are marked in red.…”

Main allergens in European hornet (<em>Vespa crabo</em> Linnaeus, 1758 ) and Asian hornet (<em>Vespa velutina </em>Lepetelier, 1836): a comparative study of their structural properties

“…Antigens 5 are proteins of unknown function in Hymenoptera venoms with high allergenic potency. In addition to Phospholipase A1, antigen 5 represents one of the most important major venom allergens in almost all allergy-relevant Vespoidea species [6].…”