Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

Blank, Simon; Seismann, Henning; Bockisch, Benjamin; Braren, Ingke; Cifuentes, Liliana; McIntyre, Mareike; Rühl, Dana; Ring, Johannes; Bredehorst, Reinhard; Ollert, Markus; Grünwald, Thomas; Spillner, Edzard

doi:10.4049/jimmunol.0803709

Cited by 110 publications

(112 citation statements)

References 55 publications

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“…In addition to the presence of CCD-sIgE in patient sera, in vitro venom double positivity can also be based on partial sequence identity of venom (glyco)proteins, for example, hyaluronidases or dipeptidyl peptidases [11,12,26], or true independent co-sensitizations to YJV and HBV. Importantly, the presence of CCD-sIgE in patients with double positive sIgE does not exclude true co-sensitization which would necessitate SIT with both venoms, whereas in the case of double positivity due to cross-reactions alone (CCD and/or peptide dependent), SIT with the primarily responsible venom would be sufficient [3].…”

Section: Discussionmentioning

confidence: 99%

Suitability of Different Glycoproteins and Test Systems for Detecting Cross-Reactive Carbohydrate Determinant-Specific IgE in Hymenoptera Venom-Allergic Patients

Mertens

2011

Int Arch Allergy Immunol

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Background: In hymenoptera venom allergy, about 75% of detected in vitro double positivity to yellow jacket and honeybee venom is ascribed to specific IgE (sIgE) directed against cross-reactive carbohydrate determinants (CCDs). To date, for the detection of CCD-sIgE, different carbohydrate antigens and methods are used. The most suitable one still has to be identified. Methods: Eighty-seven patients with confirmed hymenoptera venom allergy and venom sIgE values of ≧0.7 kU/l were investigated. Sixty-five patients showed sIgE reactivity to both yellow jacket and honeybee venom, 22 were venom mono positive and served as controls. Occurrence of CCD-sIgE was determined using bromelain, horseradish peroxidase (HRP) and MUXF³ on system A, and ascorbic acid oxidase (AAO), bromelain and HRP on system B. Further, a reference standard for CCD-sIgE evaluation was created: CCD positivity was assumed when at least 4 of the 6 test results were positive. Results: According to the defined reference standard, 45/65 venom double positive patients exhibited CCD-sIgE. Using system A, comparison with the reference standard revealed sensitivity and specificity values of 96 and 97%, respectively, for MUXF³, 100 and 100%, respectively, for bromelain, and 96 and 97%, respectively, for HRP. Using system B, sensitivity and specificity was 98 and 97%, respectively, for AAO, 62 and 95%, respectively, for bromelain, and 96 and 69%, respectively, for HRP. Results of the 3 test allergens obtained with system A showed strong correlations (r = 0.932–0.976), whereas results with system B showed lower correlations (r = 0.714–0.898). Conclusions: All 3 test allergens used with system A are suitable for CCD-sIgE detection in hymenoptera venom allergy. With system B, only AAO seems to be a reliable tool.

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Section: Discussionmentioning

confidence: 99%

Suitability of Different Glycoproteins and Test Systems for Detecting Cross-Reactive Carbohydrate Determinant-Specific IgE in Hymenoptera Venom-Allergic Patients

Mertens

2011

Int Arch Allergy Immunol

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“…There may also be cross-reactivity between homologous allergens from different species [14,38] if they partially share their identity, as is the case with hyaluronidase (Api m 2/ Ves v 2), dipeptidylpeptidase IV (Api m 5/Ves v 3), and vitellogenin (Api m 12/Ves v 6). The relevance of these crossreactions remains unknown, and further studies are needed to clarify the issue.…”

Section: Multiple Sensitizations To Hymenoptera Venomsmentioning

confidence: 99%

“…Melittin also makes it possible to distinguish between 2 forms of allergy to bee venom [12]. Other relatively scarce proteins that have been reported to be potentially allergenic are acid phosphatase (Api m 3) [8,13], dipeptidylpeptidase IV (Api m 5) [14], and icarapin (Api m 10), a complex protein with various isoforms [15]. Icarapin is a real allergen of bee venom of great diagnostic interest that could be under-represented in some therapeutic extracts [8,16].…”

Section: Latest Advances In the Molecular Diagnosis Of Insect Venom Amentioning

confidence: 99%

“…The hyaluronidases (Pol d 2 and Ves v 2) are minor allergens and, given their similarity with bee hyaluronidase (Api m 2) [20], especially through carbohydrate determinants [21], may contribute to the double positivity observed between bees and wasps. Other potentially relevant allergens are protease in Polistes (Pol d 4) and dipeptidylpeptidase IV (Ves v 3) and vitellogenin (Ves v 6) in Vespula, which exhibit partial identity with the bee allergens dipeptidylpeptidase IV (Api m 5) and vitellogenin (Api m 12), respectively [14,22].…”

Section: Latest Advances In the Molecular Diagnosis Of Insect Venom Amentioning

confidence: 99%

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Key Issues in Hymenoptera Venom Allergy: An Update

Alfaya

Soriano-Gomis

Mera

et al. 2017

J Investig Allergol Clin Immunol

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In this review, the Hymenoptera Allergy Committee of the SEAIC analyzes the most recent scientific literature addressing problems related to the diagnosis of hymenoptera allergy and to management of venom immunotherapy. Molecular diagnosis and molecular risk profiles are the key areas addressed. The appearance of new species of hymenoptera that are potentially allergenic in Spain and the associated diagnostic and therapeutic problems are also described. Finally, we analyze the issue of mast cell activation syndrome closely related to hymenoptera allergy, which has become a new diagnostic challenge for allergists given its high prevalence in patients with venom anaphylaxis.

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“…The observed association between Ac and Polistes or Vespula extract hypersensitivity was no longer present when IgE to vespid species-specific components (Ves v 1, Ves v 5 or Pol d 5) were measured. An explanation for this apparent discrepancy could be the co-recognition of cross-reactive components such as dipeptidyl-peptidase IV (Api m 5 in bee venom and Ves v 3 in wasp) or hyaluronidase (Api m 2 in bee and Ves v 2 in wasp) [10, 11]. Accordingly, a 44-kD protein similar to hyaluronidase has been already demonstrated in mosquito extracts [12].…”

mentioning

confidence: 99%

<b><i>Aedes communis</i></b> Reactivity Is Associated with Bee Venom Hypersensitivity: An in vitro and in vivo Study

Scala

Pirrotta

Uasuf

et al. 2018

Int Arch Allergy Immunol

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Mosquito bite is usually followed by a local reaction, but severe or systemic reaction may, in rare cases, occur. Allergic reactions to Aedes communis (Ac) may be underestimated due to the lack of reliable diagnostic tools. In this multicenter study, 205 individuals reporting large local reactions to Ac were enrolled and studied for cutaneous or IgE reactivity to Ac, Blattella germanica, Penaeus monodon, and Dermatophagoides pteronyssinus. Extract and molecular IgE reactivity to bees, wasps, hornets, and yellow jacket venoms were also studied in 119 patients with a clinical history of adverse reaction to Hymenoptera. Immunoblot (IB) analysis and immunoCAP IgE inhibition experiments were carried out in selected sera. Ac sensitization was recorded in 96 (46.8%) patients on SPT. Strict relationship between Ac and D. pteronyssinus, B. germanica, P. monodon, or Apis mellifera reactivity on SPT was observed. Ac IgE recognition was seen in 60/131 (45.8%) patients, 49 (81.6%) of them SPT positive, and 5/14 IB reactors. Ac IgE sensitization was associated with Tabanus spp, A. mellifera, Vespula vulgaris, and Polistes dominula reactivity. A strict relationship between Ac IgE reactivity and Api m 1, Api m 2, Api m 3, Api m 5, and Api m 10 was recorded. IgE reactivity to AC was inhibited in 9/15 cases after serum absorption with the A. mellifera extract. Both SPT and IgE Ac reactivity is observed in about half of patients with a history of large local reactions to mosquito bites. The significant relationship between Ac sensitization and either extract or single bee venom components is suggestive of a “bee-mosquito syndrome” occurrence.

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Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

Cited by 110 publications

References 55 publications

Suitability of Different Glycoproteins and Test Systems for Detecting Cross-Reactive Carbohydrate Determinant-Specific IgE in Hymenoptera Venom-Allergic Patients

Suitability of Different Glycoproteins and Test Systems for Detecting Cross-Reactive Carbohydrate Determinant-Specific IgE in Hymenoptera Venom-Allergic Patients

Key Issues in Hymenoptera Venom Allergy: An Update

<b><i>Aedes communis</i></b> Reactivity Is Associated with Bee Venom Hypersensitivity: An in vitro and in vivo Study

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