Current Advances in Immunological Studies on the Vespidae Venom Antigen 5: Therapeutic and Prophylaxis to Hypersensitivity Responses

Bazon, Murilo Luiz; Silveira, Lais Helena; Simioni, Patricia Ucelli; Brochetto-Braga, Márcia Regina

doi:10.3390/toxins10080305

Cited by 15 publications

(6 citation statements)

References 104 publications

(158 reference statements)

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“…Nine wasp venom proteins ( Table 2 ) were matched with 12 screened peptides (red, Table 1 ). The nine wasp venom proteins were vitellogenin precursor [ 24 ], hexamerin 70b precursor [ 24 ], venom carboxylesterase-6 precursor [ 24 ], MRJP5 [ 25 ], major royal jelly protein 8 precursor [ 26 ], venom acid phosphatase Acph-1 precursor [ 27 ], phospholipase A2 [ 28 ], venom serine protease 34 precursor [ 6 , 24 ], and major royal jelly protein 9 precursor [ 26 ].…”

Section: Resultsmentioning

confidence: 99%

“…The composition of wasp venom was first elucidated in the 1950s when scientists discovered that it was mainly composed of amines, peptides, enzymes, and other proteins with unknown function [ 5 , 6 ]. Venom is stored in the stinger glands, in the ventral end of the wasp, and is mainly composed of serotonin, histamine, bradykinin, hyaluronidase, and a large number of peptides and proteins [ 7–9 ].…”

Section: Introductionmentioning

confidence: 99%

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Biopanning of allergens from wasp sting patients

et al. 2018

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Objective: Wasp venom is a potentially important natural drug, but it can cause hypersensitivity reactions. The purpose of the present study was to systematically study the epitopes of wasp venom. Methods: Using a random 12-peptide phage library, we performed antibody-binding epitope panning on ten serum samples from wasp sting victims at 3 h and 4 days after the sting. The panning epitopes were identified by high-throughput sequencing and matched with wasp venom proteins by BLAST. The panned antibody-binding epitopes were verified by ELISA. Results: A total of 35 specific potential wasp venom epitopes in 4 days were identified. Amongst them, twelve peptide epitopes were matched with nine wasp venom proteins, namely, vitellogenin precursor, hexamerin 70b precursor, venom carboxylesterase-6 precursor, MRJP5, major royal jelly protein 8 precursor, venom acid phosphatase Acph-1 precursor, phospholipase A2, venom serine protease 34 precursor, and major royal jelly protein 9 precursor. The changes in serum IgM antibodies induced by wasp venom were confirmed by ELISA based on the 12 peptide epitopes. Conclusion: The nine wasp venom proteins are potential allergens, which should be excluded or modified in the potential biomedical applications of wasp venom.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biopanning of allergens from wasp sting patients

et al. 2018

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“…Phospholipase A1 (Ves v 1), hyaluronidase (Ves v 2), protease vitellogenin (Ves v 6), and antigen 5 (Ves v 5) are the most allergenic components of the genera Dolichovespula, Polistes, Vespula, and Vespa [ 152 , 153 , 154 ]. Phospholipase A1, hyaluronidase, and antigen 5 are the three main allergens described for P. paulista venom and cause a high number of allergic reactions and dozens of fatal anaphylaxis cases annually in Brazil [ 155 , 156 , 157 ].…”

Section: Wasp Venom Allergies and Sensitization: A Double-edged mentioning

confidence: 99%

Wasp Venom Biochemical Components and Their Potential in Biological Applications and Nanotechnological Interventions

El-Wahed

Yosri

Sakr

et al. 2021

Toxins

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Wasps, members of the order Hymenoptera, are distributed in different parts of the world, including Brazil, Thailand, Japan, Korea, and Argentina. The lifestyles of the wasps are solitary and social. Social wasps use venom as a defensive measure to protect their colonies, whereas solitary wasps use their venom to capture prey. Chemically, wasp venom possesses a wide variety of enzymes, proteins, peptides, volatile compounds, and bioactive constituents, which include phospholipase A2, antigen 5, mastoparan, and decoralin. The bioactive constituents have anticancer, antimicrobial, and anti-inflammatory effects. However, the limited quantities of wasp venom and the scarcity of advanced strategies for the synthesis of wasp venom’s bioactive compounds remain a challenge facing the effective usage of wasp venom. Solid-phase peptide synthesis is currently used to prepare wasp venom peptides and their analogs such as mastoparan, anoplin, decoralin, polybia-CP, and polydim-I. The goal of the current review is to highlight the medicinal value of the wasp venom compounds, as well as limitations and possibilities. Wasp venom could be a potential and novel natural source to develop innovative pharmaceuticals and new agents for drug discovery.

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“…Their venom is a complex mixture of low-weight molecules, peptides and proteins, which can act as pheromones, toxins and allergens. [34][35][36][37] These compounds are synthesized, stored and secreted by the venom gland in response to various stimuli.…”

Section: The Venom Of Ve Spa Velutina Nig Rithor a Xmentioning

confidence: 99%

“…Asian wasps, as with other social Hymenoptera, have glands and a sac with venom in their abdomen. Their venom is a complex mixture of low‐weight molecules, peptides and proteins, which can act as pheromones, toxins and allergens 34–37 . These compounds are synthesized, stored and secreted by the venom gland in response to various stimuli.…”

Section: The Venom Of Vespa Velutina Nigrithoraxmentioning

confidence: 99%

The Asian wasp Vespa velutina nigrithorax: Entomological and allergological characteristics

Vidal

2021

Clin Experimental Allergy

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The Asian wasp, also known as the Asian predatory wasp or the Asian hornet (Vespa velutina, of the Vespa genus, Vespidae family and Hymenoptera order), was first described in 1836 by the French entomologist Amédée Louis Michel Lepeletier. This species of wasp originated from South-East Asia, in particular the region between Northern India and the Indochinese Peninsula, Taiwan and Indonesia. Due to its extreme success in colonizing new areas, V. velutina is now widespread in other continents and countries where it is considered an invasive species. [1][2][3][4][5][6][7][8][9][10] Although V. velutina Lepeletier 1836 is a well-defined wasp, up to 12 different colour variants geographically distributed throughout Asia have been identified. 11 These colouration patterns and their geographic variations are determined by genes, as have been proven with specific mitochondrial and microsatellite markers; however, the influence of developmental constraints related to crypsis, thermoregulation and aposematism has also been suggested. 11 In general, variations in colouration are a genuine visual aposematic signal that species employ to warn potential predators as a defence against being attacked or eaten. The warning signals displayed by wasps include the colour patterns of the various body segments, using light and black stripes on the abdomen, with yellow, red, black and white the most effective colours. The coloration of V. velutina varies among populations from almost entirely yellow or orange to extensively black. 12,13

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Current Advances in Immunological Studies on the Vespidae Venom Antigen 5: Therapeutic and Prophylaxis to Hypersensitivity Responses

Cited by 15 publications

References 104 publications

Biopanning of allergens from wasp sting patients

Biopanning of allergens from wasp sting patients

Wasp Venom Biochemical Components and Their Potential in Biological Applications and Nanotechnological Interventions

The Asian wasp Vespa velutina nigrithorax: Entomological and allergological characteristics

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