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Toxins
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Advances in Venom Immunology and Allergy
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Advances in Venom Immunology and Allergy

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 6456

Special Issue Editors

Dr. Aurora Jurado

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Guest Editor
UGC Inmunología-Alergología, Maimonides Biomedical Research Institute of Cordoba (IMIBIC), Reina Sofia University Hospital, University of Cordoba, 14004 Cordoba, Spain
Interests: allergy; autoimmunity; therapeutic nanoparticles
Dr. Carmen Moreno-Aguilar

E-Mail Website
Guest Editor
UGC Inmunología-Alergología, Maimonides Biomedical Research Institute of Cordoba (IMIBIC), Reina Sofia University Hospital, University of Cordoba, 14004 Cordoba, Spain
Interests: allergy; anaphylaxis
Dr. Berta Ruiz-León

E-Mail Website
Guest Editor
UGC Inmunología-Alergología, Maimonides Biomedical Research Institute of Cordoba (IMIBIC), Reina Sofia University Hospital, University of Cordoba, 14004 Cordoba, Spain
Interests: allergy; hymenoptera venom allergy

Special Issue Information

Dear Colleagues,

Allergy to Hymenoptera venom is a life-threatening condition, often going underdiagnosed because of the general population's poor knowledge concerning the condition and many sanitary actors. It has been established that IgE-mediated hypersensitivity is triggered by allergenic proteins in the venom of social bees and wasps, resulting in the massive liberation of acute inflammatory mediators. These produce an increased capillary permeability, extravasation and hypotension, bronchoconstriction and hypoxia that can produce heart, brain, lung and kidney failure, accompanied by skin pruritus and oedema and generalized gland dysfunction.

In recent years, some allergenic proteins from Apis mellifera, Bombus Terrestris, and some species of wasps belonging to Vespula, Vespa, Dolichovespula and Polistes genera have been characterized.

A variable degree of molecular similarities among proteins could be responsible for the cross-reactivity and presence of glycosylated radicals.

Up till now, the most critical risk factor for developing an allergy to Hymenoptera venom appeared to be the high degree of exposure of people working in beekeeping, trucking and farming, in addition to people frequent performing outdoor activities.

Venom immunotherapy is the only way to redirect the failure of immune tolerance underlying venom-allergic individuals.

Our focus is to analyse 1) the entomological aspects of allergenic Hymenoptera and its interaction with the human habitat, 2) novel allergenic molecules from Hymenoptera venom and their relevance considering both the disease and the therapeutic value of the extracts for vaccines, 3) the underlying immune mechanisms of the disease, including predictive risk and severity factors, 4) and the therapeutic mechanisms of vaccination, including the chronology of the effect during active treatment and after discontinuation.

Dr. Aurora Jurado
Dr. Carmen Moreno-Aguilar
Dr. Berta Ruiz-León
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Hymenoptera venom allergy
  • allergy to stings
  • bee venom allergy
  • wasp venom allergy
  • anaphylaxis
  • tolerance to Hymenoptera venom
  • Hymenoptera venom allergenic proteins
  • Hymenoptera venom immunotherapy

Published Papers (3 papers)

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Research

7 pages, 663 KiB  
Communication
Hymenoptera Allergy Diagnosis through Their Presence on Human Food
by Arantza Vega-Castro, Leopoldo Castro, Francisco Carballada, Teresa Alfaya, Lluís Marquès and Berta Ruíz-León
Toxins 2023, 15(12), 680; https://doi.org/10.3390/toxins15120680 - 1 Dec 2023
Viewed by 1351
Abstract
Venom immunotherapy (VIT) protects up to 98% of treated Hymenoptera allergy patients from reactions with new stings. A correct diagnosis with the identification of the venom causing the allergic reaction is essential to implementing it. The knowledge of the Hymenoptera foraging habits when [...] Read more.
Venom immunotherapy (VIT) protects up to 98% of treated Hymenoptera allergy patients from reactions with new stings. A correct diagnosis with the identification of the venom causing the allergic reaction is essential to implementing it. The knowledge of the Hymenoptera foraging habits when the sting takes place in a food environment would allow the culprit insect to be known. Images of Hymenoptera occurring in environments where there was human food were recorded in Spain, including the date of the image, the place description and its geolocation. The insects’ genus and species were identified by an entomologist. Results: One hundred and fifty-five images depicting 71 insects were analyzed. The identified insects were Vespula (56), Vespa (7), Polistes (4), Cerceris (2), Bombus (1) and Apis (1). Most (97.1%) of the images were obtained in summer and early autumn, outdoors in terraces (64%). Meat was the food associated with 47.9% of the images. In protein-rich foods, Vespula was found in 89%. Conclusions: Vespula was the main Hymenoptera associated with food environments in our country (78.87%), and in most of the cases (71%), the food involved is a source of protein, such as meat or seafood. In that environment, the probability that the insect is a Vespula would be 89%. Full article
(This article belongs to the Special Issue Advances in Venom Immunology and Allergy)
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16 pages, 2958 KiB  
Article
Structural Similarities, in Relation with the Cross-Reactivity, of Hymenoptera Allergenic Dipeptidyl Peptidases IV—An Overall Comparison Including a New Dipeptidyl Peptidase IV Sequence from Vespa velutina
by Rafael I. Monsalve, Manuel Lombardero, Lars H. Christensen, Beatriz Núñez-Acevedo, David González-de-Olano, Miriam Sobrino-García, Rosita M. Castillo-Loja, Susana B. Bravo, Manuela Alonso-Sampedro and Carmen Vidal
Toxins 2023, 15(11), 656; https://doi.org/10.3390/toxins15110656 - 14 Nov 2023
Viewed by 1150
Abstract
(1) Background: Dipeptidyl Peptidases IV (DPPIVs), present in many organisms, are minor components in the venoms of Hymenoptera, where they have been identified as cross-reactive allergenic molecules. Considering that the structure of homologous DPPIVs is well characterized, we aimed to explain which regions [...] Read more.
(1) Background: Dipeptidyl Peptidases IV (DPPIVs), present in many organisms, are minor components in the venoms of Hymenoptera, where they have been identified as cross-reactive allergenic molecules. Considering that the structure of homologous DPPIVs is well characterized, we aimed to explain which regions have higher similarity among these proteins and present a comparison among them, including a new Vespa velutina DPPIV sequence. Moreover, two cases of sensitization to DPPIVs in wasp- and honeybee-sensitized patients are presented. (2) Methods: Proteomic analyses have been performed on the venom of the Asian hornet Vespa velutina to demonstrate the sequence of its DPPIV (allergen named Vesp v 3, with sequence accession number P0DRB8, and with the proteomic data available via ProteomeXchange with the identifier PXD046030). A comparison performed through their alignments and analysis of the three-dimensional structure showed a region with higher similarity among Hymenoptera DPPIVs. Additionally, ImmunoCAP™ determinations (including specific inhibition experiments), as well as IgE immunoblotting, are performed to demonstrate the allergenicity of Api m 5 and Ves v 3. (3) Results and Conclusions: The data presented demonstrate that the similarities among Hymenoptera DPPIVs are most likely localized at the C-terminal region of these enzymes. In addition, a higher similarity of the Vespa/Vespula DPPIVs is shown. The clinical cases analyzed demonstrated the allergenicity of Api m 5 and Ves v 3 in the sera of the allergic patients, as well as the presence of this minor component in the preparations used in venom immunotherapy. Full article
(This article belongs to the Special Issue Advances in Venom Immunology and Allergy)
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17 pages, 2908 KiB  
Article
Proteomics of Vespa velutina nigrithorax Venom Sac Queens and Workers: A Quantitative SWATH-MS Analysis
by Manuela Alonso-Sampedro, Xesús Feás, Susana Belén Bravo, María Pilar Chantada-Vázquez and Carmen Vidal
Toxins 2023, 15(4), 266; https://doi.org/10.3390/toxins15040266 - 3 Apr 2023
Cited by 3 | Viewed by 3430
Abstract
Health risks caused by stings from Vespa velutina nigrithorax (VV), also known as the yellow-legged Asian hornet, have become a public concern, but little is known about its venom composition. This study presents the proteome profile of the VV’s venom sac (VS) based on [...] Read more.
Health risks caused by stings from Vespa velutina nigrithorax (VV), also known as the yellow-legged Asian hornet, have become a public concern, but little is known about its venom composition. This study presents the proteome profile of the VV’s venom sac (VS) based on Sequential Window Acquisition of all Theoretical Mass Spectra (SWATH-MS). The study also performed proteomic quantitative analysis and examined the biological pathways and molecular functions of the proteins in the VS of VV gynes (i.e., future queens [SQ]) and workers [SW]. The total protein content per VS was significantly higher in the SW than in the SQ (274 ± 54 µg/sac vs. 175 ± 22 µg/sac; p = 0.02). We quantified a total of 228 proteins in the VS, belonging to 7 different classes: Insecta (n = 191); Amphibia and Reptilia (n = 20); Bacilli, γ-Proteobacteria and Pisoniviricetes (n = 12); and Arachnida (n = 5). Among the 228 identified proteins, 66 showed significant differential expression between SQ and SW. The potential allergens hyaluronidase A, venom antigen 5 and phospholipase A1 were significantly downregulated in the SQ venom. Full article
(This article belongs to the Special Issue Advances in Venom Immunology and Allergy)
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