Dipeptidyl peptidase IV of the Vespa velutina nigrithorax venom is recognized as a relevant allergen

Pretre, Gabriela; Asturias, J A; Lizaso, María Teresa; Tabar, A. I.

doi:10.1016/j.anai.2022.02.018

Cited by 4 publications

(13 citation statements)

References 34 publications

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“…Recently, it has been found to participate in the hydrolysis of dietary gliadin, which is rich in proline residues, performing a digestive function in the larval gut of T. molitor [ 3 ]. As a venom component of the honey bee, hornet, and paper wasp, DPPIV was characterized as an allergen, and may be involved in processing peptidic toxins [ 12 , 13 , 14 , 15 , 16 , 17 ]. Venom of these wasps commonly causes allergic reactions among humans, and is used to defend their colonies from vertebrate predators; this is different from the venom of parasitoids, which is responsible for paralyzing hosts and manipulating their parasitized hosts for the survival and development of their progeny [ 21 , 36 , 37 , 38 ].…”

Section: Discussionmentioning

confidence: 99%

“…Compared with mammalian DPPIV, little is known about insect DPPIV, with information derived from limited studies conducted on a few species, including blue blowfly Calliphora vicina [ 9 ], cockroach Leucophaea maderae [ 10 ], fruit fly Drosophila melanogaster [ 11 ], yellow mealworm Tenebrio molitor [ 3 ], honey bee Apis mellifera [ 12 ], and several wasps [ 12 , 13 , 14 , 15 , 16 , 17 ]. Insect DPPIV was first partially purified from C. vicina , which has been shown to be able to degrade the ecdysiostatic peptide, i.e., trypsin-modulating oostatic factor, of the grey flesh fly Neobellieria bullata [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

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Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the Ectoparasitoid Scleroderma guani

Yang

Wang

et al. 2023

Toxins

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Dipeptidyl peptidase IV (DPPIV) is a proline-specific serine peptidase that remains poorly investigated in terms of venom composition. Here, we describe the molecular characteristics and possible functions of DPPIV as a major venom component of the ant-like bethylid ectoparasitoid, Scleroderma guani, named SgVnDPPIV. The SgVnDPPIV gene was cloned, which encodes a protein with the conserved catalytic triads and substrate binding sites of mammalian DPPIV. This venom gene is highly expressed in the venom apparatus. Recombinant SgVnDPPIV, produced in Sf9 cells using the baculovirus expression system, has high enzymatic activity, which can be efficiently inhibited by vildagliptin and sitagliptin. Functional analysis revealed that SgVnDPPIV affects genes related to detoxification, lipid synthesis and metabolism, response to stimuli, and ion exchange in pupae of Tenebrio molitor, an envenomated host of S. guani. The present work contributes towards understanding the role of venom DPPIV involved in the interaction between parasitoid wasp and its host.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the Ectoparasitoid Scleroderma guani

Yang

Wang

et al. 2023

Toxins

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“…Recently two new allergens (dipeptidyl peptidase IV and serin protease) have been identified in the VV venom. 59 Due to the high similarity between all hornet venoms, cross-reactivity of (sub)tropical Vespa species with Vespula may be expected to be comparable to that of Vespa crabro .…”

Section: Bumblebee Allergens and Cross-reactivity With Honey Beementioning

confidence: 99%

Allergy to stings and bites from rare or locally important arthropods: worldwide distribution, available diagnostics, and treatment

Arzt‐Gradwohl

Sturm

Boni

et al. 2023

Preprint

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Insect venom allergy is the most frequent cause of anaphylaxis in Europe and possibly worldwide. The majority of systemic allergic reactions after insect stings are caused by Hymenoptera and among these, vespid genera induce most of the systemic sting reactions (SSR). Honey bees are the second leading cause of SSR. Depending on the global region, other Hymenoptera such as different ant genera are responsible for SSR. Widely distributed hornets and bumblebees or local vespid or bee genera rarely induce SSR. Hematophagous insects such as mosquitoes and horse flies usually cause (large) local reactions while SSR occasionally occur. This position paper aims to identify either rare or locally important insects causing SSR as well as rarely occurring SSR after stings or bites of widely distributed insects. We summarized relevant venom or saliva allergens and intended to identify possible cross-reactivities between the insect allergens. Moreover, we aimed to locate diagnostic tests for research and routine diagnosis, which are sometimes only regionally available. Finally, we gathered information on disposable immunotherapies. Major allergens of most insects were identified, and cross-reactivity between insects was frequently observed. While some diagnostics and immunotherapies are locally available, standardized skin tests and immunotherapies are generally lacking in rare insect allergy.

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“…Recently, two new allergens (dipeptidyl peptidase IV and serin protease) have been identified in the VV venom. 59 Due to the high similarity between all hornet venoms, crossreactivity of (sub)tropical Vespa species with Vespula may be expected to be comparable to that of Vespa crabro. ants) (Table 3).…”

Section: Cross-reactivity Of Vespa Venomsmentioning

confidence: 99%

“…Hornet PLAs1 share 65%–70% SI with each other. Recently, two new allergens (dipeptidyl peptidase IV and serin protease) have been identified in the VV venom 59 …”

Section: Cross‐reactivitymentioning

confidence: 99%

Allergy to stings and bites from rare or locally important arthropods: Worldwide distribution, available diagnostics and treatment

Sturm

Boni

Antolín‐Amérigo

et al. 2023

Allergy

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Dipeptidyl peptidase IV of the Vespa velutina nigrithorax venom is recognized as a relevant allergen

Cited by 4 publications

References 34 publications

Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the Ectoparasitoid Scleroderma guani

Molecular Characterization and Functional Analysis of the Dipeptidyl Peptidase IV from Venom of the Ectoparasitoid Scleroderma guani

Allergy to stings and bites from rare or locally important arthropods: worldwide distribution, available diagnostics, and treatment

Allergy to stings and bites from rare or locally important arthropods: Worldwide distribution, available diagnostics and treatment

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