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Natural and Induced Tolerance to Hymenoptera Venom: A Single Mechanism?

ABSTRACT: Inducing tolerance in Hymenoptera-allergic patients, bee venom immunotherapy (BVIT) is a widely accepted method to treat severe allergy to bee stings. In order to increase the existing knowledge on the underlying immunological mechanisms and look for possible biomarkers predictive of efficacy, a group of 20 bee-venom-allergic patients (AG) were thoroughly examined during their first year of BVIT. In addition, the results of treated patients with those of an untreated group of 20 tolerant beekeepers (TG) who had previously shown a firm suppressor-regulatory profile were compared. Tolerance in AG patients was invariably associated with a significant regulatory response characterised by the expansion of Helios^- subpopulation and increased IL-10, specific IgG4 (sIgG4), and kynurenine levels. Although specific IgE (sIgE) levels increased transiently, surprisingly, the T helper type 2 (Th2) population and IL-4 levels rose significantly after one year of immunotherapy. Thus, the picture of two parallel phenomena emerges: a tolerogenic response and an allergenic one. Comparing these results with those obtained from the TG, different immunological mechanisms appear to govern natural and acquired tolerance to immunotherapy. Of particular interest, the kynurenine levels and T regulatory (Treg) Helios^- population could be proposed as new biomarkers of response to BVIT.

SUBMITTER: Navas A

PROVIDER: S-EPMC9320229 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Single-cell profiling reveals novel cellular heterogeneity of monocytes during Hymenoptera venom allergy.

Project description:BackgroundHymenoptera stings can induce dysregulated inflammation and immediate hypersensitivity reactions including anaphylaxis. However, the molecular mechanisms underlying peripheral immune responses during Hymenoptera venom allergy (HVA) remain elusive.MethodsHere we determined the single-cell transcriptomic profiling from highly heterogeneous peripheral blood cells in patients with HVA through unbiased single-cell RNA sequencing and multiple models of computational analyses.ResultsThrough clustering analysis by uniform manifold approximation and projection, we revealed an increased number of monocytes in the acute phase and identified innate immune responses, leukocyte activation, and cellular detoxification as the main involved biological processes. We used filter analysis to identify that CLU that encodes clusterin was highly expressed in monocytes, and the co-expressed genes of CLU further supported the key role of monocyte. We further used pseudo-temporal ordering of cells and scRNA velocity analysis to delineate disease-associated monocyte lineages and states in patients with HVA.ConclusionsOur comprehensive molecular profiling of blood samples from patients with HVA revealed previously unknown molecular changes, providing important insights into the mechanism of venom allergy and potential therapeutic targets.

| S-EPMC9069361 | biostudies-literature

Hymenoptera venom allergy: work disability and occupational impact of venom immunotherapy.

Project description:ObjectivesLittle is known about the Hymenoptera venom allergy impact on work ability and the effect of venom immunotherapy (VIT) on work. The objective of this study was to evaluate the prevalence and predictors of work disability in patients treated with VIT and the effects of VIT on occupational functioning.Methods181 patients, aged 18-71 years, treated with VIT while working, were investigated by questionnaire. Participants were classified into employed and self-employed and, based on work exposure to Hymenoptera, into three risk categories: high risk, occasionally high risk and low risk. Work disability was defined as having to have changed jobs/tasks and/or suffered economic loss because of Hymenoptera venom allergy. Predictors of work disability were assessed in logistic regression models.Results31 (17%) patients reported work disability. Being self-employed and having the severe reaction at work were associated with work disability (p<0.01). Having a high-risk job for exposure to Hymenoptera was a significant predictor of work disability (OR 2.66, 95% CI 1.04 to 6.75). 24% of patients referred a positive effect of VIT on work. Determinants of the positive effect of VIT on work were having a high-risk job for exposure to hymenoptera (OR 3.60, 95% CI 1.52 to 8.51) and having already concluded VIT (OR 2.82, 95% CI 1.30 to 6.14).ConclusionsHymenoptera venom allergy could determine work disability. Patients with Hymenoptera venom allergy having a high-risk job for exposure to Hymenoptera seem to have higher risk of work disability and refer more frequently a positive effect of VIT on work.

| S-EPMC4127938 | biostudies-literature

Proteo-Transcriptomic Characterization of Sirex nitobei (Hymenoptera: Siricidae) Venom.

Project description:The wood-boring woodwasp Sirex nitobei is a native pest in Asia, infecting and weakening the host trees in numerous ecological and commercial coniferous forest plantations. In China, hosts of S. nitobei are diverse, so the pest has spread to several provinces of China, resulting in considerable economic and ecological damage. During female oviposition, S. nitobei venom along with arthrospores of the symbiotic fungus Amylostereum areolatum or A. chaetica is injected into host trees, and the combination of these two biological factors causes the death of xylem host trees. The presence of venom alone causes only the yellowing and wilting of needles. In this study, we constructed the venom gland transcriptome of S. nitobei for the first time and a total of 15,036 unigenes were acquired. From the unigenes, 11,560 ORFs were identified and 537 encoding protein sequences with signal peptides at the N-terminus. Then, we used the venomics approach to characterize the venom composition of female S. nitobei and predicted 1095 proteins by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. We focused on seven proteins that were both highly expressed in the venom gland transcriptome and predicted in the crude venom proteome. These seven proteins are laccase-2, laccase-3, a protein belonging to the Kazal family, chitooligosaccharidolytic β-N-acetylglucosaminidase, beta-galactosidase, icarapin-like protein, and waprin-Thr1-like protein. Using quantitative real-time PCR (qRT-PCR), we also proved that the genes related to these seven proteins are specifically expressed in the venom glands. Finally, we revealed the functional role of S. nitobei venom in the physiological response of host trees. It can not only promote the colonization of symbiotic fungus but contribute to the development of eggs and larvae. This study provides a deeper understanding of the molecular mechanism of the woodwasp-pine interaction.

| S-EPMC8402507 | biostudies-literature

Proteomic features characterization of <i>Hymenoptera</i> venom allergy.

Project description:BackgroundHymenoptera venom allergy is one of the most frequent causes of anaphylaxis. In its most severe form, the reaction to wasp and honey bee stings may be life-threatening. Therefore, immediate and proper diagnosis of venom allergy and implementation of suitable therapy are extremely important. Broadening the knowledge on the mechanism of the allergic reaction may contribute to the improvement of both diagnostic and treatment methods. Thus, this study aimed to discover changes in protein expression in serum of patients allergic to Hymenoptera (wasp and honeybee) venom and to point out proteins and peptides involved in the allergic inflammation.MethodsSerum proteomic patterns typical to allergic patients and healthy volunteers were obtained with MALDI-TOF (matrix-assisted laser desorption/ionization-time of flight) mass spectrometer. The spectra were processed, analyzed and compared using advanced bioinformatics tools. The discriminative peaks were subjected to identification with liquid chromatography coupled with tandem mass spectrometry.ResultsThis methodology allowed for the identification of four features differentiating between allergy and control groups. They were: fibrinogen alpha chain, coagulation factor XIII chain A, complement C4-A, and inter-alpha-trypsin inhibitor heavy chain H4. All of these proteins are involved in allergic inflammatory response.ConclusionsExtending the knowledge of the Hymenoptera venom sensitization will contribute to the development of novel, sensitive and specific methods for quick and unambiguous allergy diagnosis. Understanding the basis of the allergy at the proteomic level will support the improvement of preventive and therapeutic measures.

| S-EPMC6881982 | biostudies-literature

A new cytogenetic mechanism for bacterial endosymbiont-induced parthenogenesis in Hymenoptera.

Project description:Vertically transmitted endosymbiotic bacteria, such as Wolbachia, Cardinium and Rickettsia, modify host reproduction in several ways to facilitate their own spread. One such modification results in parthenogenesis induction, where males, which are unable to transmit the bacteria, are not produced. In Hymenoptera, the mechanism of diploidization due to Wolbachia infection, known as gamete duplication, is a post-meiotic modification. During gamete duplication, the meiotic mechanism is normal, but in the first mitosis the anaphase is aborted. The two haploid sets of chromosomes do not separate and thus result in a single nucleus containing two identical sets of haploid chromosomes. Here, we outline an alternative cytogenetic mechanism for bacterial endosymbiont-induced parthenogenesis in Hymenoptera. During female gamete formation in Rickettsia-infected Neochrysocharis formosa (Westwood) parasitoids, meiotic cells undergo only a single equational division followed by the expulsion of a single polar body. This absence of meiotic recombination and reduction corresponds well with a non-segregation pattern in the offspring of heterozygous females. We conclude that diploidy in N. formosa is maintained through a functionally apomictic cloning mechanism that differs entirely from the mechanism induced by Wolbachia.

| S-EPMC2605818 | biostudies-literature

Platelet-activating factor acetylhydrolase: A biomarker in Hymenoptera venom allergy?

Project description: Not available

| S-EPMC9299147 | biostudies-literature

Recombinant phospholipase A1 (Ves v 1) from yellow jacket venom for improved diagnosis of hymenoptera venom hypersensitivity.

Project description:BackgroundHymenoptera venoms are known to cause life-threatening IgE-mediated anaphylactic reactions in allergic individuals. Proper diagnosis of hymenoptera venom allergy using venom extracts is severely affected by molecular cross-reactivities. Although non-glycosylated marker allergens would facilitate the identification of the culprit venom, the major allergen phospholipase A1 (Ves v 1) from yellow jacket venom (YJV) remained unavailable so far.MethodsExpression of Ves v 1 as wild type and enzymatically inactivated mutant and Ves v 5 in insect cells yielded soluble proteins that were purified via affinity chromatography. Functionality of the recombinant allergens was assessed by enzymatic and biophysical analyses as well as basophil activation tests. Diagnostic relevance was addressed by ELISA-based analyses of sera of YJV-sensitized patients.ResultsBoth major allergens Ves v 1 and Ves v 5 could be produced in insect cells in secreted soluble form. The recombinant proteins exhibited their particular biochemical and functional characteristics and were capable for activation of human basophils. Assessment of IgE reactivity of sera of YJV-sensitized and double-sensitized patients emphasised the relevance of Ves v 1 in hymenoptera venom allergy. In contrast to the use of singular molecules the combined use of both molecules enabled a reliable assignment of sensitisation to YJV for more than 90% of double-sensitised patients.ConclusionsThe recombinant availability of Ves v 1 from yellow jacket venom will contribute to a more detailed understanding of the molecular and allergological mechanisms of insect venoms and may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy.

| S-EPMC2867971 | biostudies-literature

Development of children's hymenoptera venom allergy quality of life scale (CHVAQoLS).

Project description:BackgroundVenom allergy is a rare but life-threatening disease and may have a considerable impact on the health-related quality of life (HRQoL) of patients, especially children. This paper presents development of the HRQoL scale for children and adolescents with Hymenoptera venom allergy (HVA).MethodsThe study sample consisted of 71 children, born between 1992 and 2000, who presented with a history of insect sting reaction when referred for consultation in the allergy center of Polish-American Children's Hospital, Krakow, Poland, during the period from 2000 to 2010. The initial pool of 60 items - divided into 6 domains - was prepared. The items with intercorrelations higher than 0.7 were removed from each domain and then principal component analysis was conducted for each domain separately, to provide a one-dimensional subscale for each domain. Reliability of the subscales was assessed using Cronbach alpha coefficient in terms of Classical Test Theory and with rho coefficient in terms of Item Response Theory. The multidimensionality of the scale was tested using multi-trait scaling.ResultsThree to four items from each domain were subsequently selected to constitute six subscales. Rho coefficients for all the subscales reached 0.8, similar results were achieved with the Cronbach alpha coefficients. Multi-trait method showed that the majority of the items indicated stronger correlations with their own subscales than with other subscales, which proves that our constructed subscales measure different dimensions of HRQoL.ConclusionsThe presented scale comprises high validity and reliability subscales measuring six dimensions of HRQoL related to Hymenoptera venom allergy in children and adolescents. Such information may be useful in everyday clinical practice.

| S-EPMC3750314 | biostudies-literature

Lysiphlebus fabarum (Hymenoptera: Braconidae: Aphidiinae) venom proteomic analysis

Project description:Venom injected at oviposition is crucial for successful reproduction in most parasitoid wasp species (Moreau & Asgari 2015; Poirié et al. 2014). The venom of the pea aphid parasitoid Aphidius ervi was analyzed previously using a combined transcriptomic and proteomic approach (Colinet et al. 2014) and we applied similar methods here to compare the venom composition in Lysiphlebus fabarum, that also used the pea aphid as host. Venom was extracted from the L. fabarum venom gland and analyzed using 1D gel electrophoresis and mass spectrometry. A total of 35 L. fabarum proteins were identified as putative venom proteins using these results combined with available transcriptomic data (Dennis et al. 2017) and the genomic data.

2020-04-24 | PXD015758 | Pride

Venom Function of a New Species of Megalomyrmex Forel, 1885 (Hymenoptera: Formicidae).

Project description:Alkaloids are important metabolites found across a variety of organisms with diverse ecological functions. Of particular interest are alkaloids found in ants, organisms well known for dominating the ecosystems they dwell in. Within ants, alkaloids are found in venom and function as potent weapons against heterospecific species. However, research is often limited to pest species or species with parasitic lifestyles and thus fails to address the broader ecological function of ant venom alkaloids. Here we describe a new species of free-living Megalomyrmex ant: Megalomyrmex peetersi sp. n. In addition, we identify its singular venom alkaloid (trans-2-butyl-5-heptylpyrrolidine) and elucidate the antibiotic and insecticidal functions of its venom. Our results show that Megalomyrmex peetersi sp. n. venom is an effective antibiotic and insecticide. These results are comparable to venom alkaloids found in other ant species, such as Solenopsis invicta. This research provides great insight into venom alkaloid function, and it is the first study to explore these ideas in the Megalomyrmex system.

| S-EPMC7693960 | biostudies-literature

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