Biopanning of allergens from wasp sting patients

Chai, Limin; Yang, Xia; Liu, Mei; Liu, Chunyan; Han, Limei; Guo, Hui; Li, Changsheng; Sun, Yuhui; Li, Xiaoyan; Xiao, Min; Fang, Zhicheng

doi:10.1042/bsr20181113

Cited by 8 publications

(6 citation statements)

References 42 publications

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“…In Clade E, there is a relatively independent group with 1:1:1:1:1:1 orthology ( Hpbe1 / Hcbe9 / Dmbe1 / Tcbe1 / Tmbe1 / Avbe17 ) across species. These β‐esterases have all been predicted as venom COE, which has different functions, such as an allergen in hymenopteran insects (Chai et al, 2018), and an odorant degrading enzyme (Dmbe2: CG6917) in the D. melanogaster olfactory sensilla (Chertemps et al, 2012). However, the six β‐esterases ( Hpbe1 / Hcbe9 / Dmbe1 / Tcbe1 / Tmbe1 / Avbe17 ) identified in our study have low identity with Dmbe2 .…”

Section: Resultsmentioning

confidence: 99%

Comparative genomic analysis of carboxylesterase genes in Tenebrio molitor and other four tenebrionids

Yang

Wang

et al. 2022

Arch Insect Biochem Physiol

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Carboxylesterases (COEs) have various functions in wide taxons of organisms. In insects, COEs are important enzymes involved in the hydrolysis of a variety of estercontaining xenobiotics, neural signal transmission, pheromone degradation, and reproductive development. Understanding the diversity of COEs is basic to illustrate their functions. In this study, we identified 53, 105, 37, and 39 COEs from the genomes of Tenebrio molitor, Asbolus verucosus, Hycleus cichorii, and H. phaleratus in the superfamily of Tenebrionidea, respectively. Phylogenetic analysis showed that 234 COEs from these four species and those reported in Tribolium castaneum (63) could be divided into 12 clades and three major classes. The αesterases significantly expanded in T. molitor, A. verucosus, and T. castaneum compared to dipteran and hymenopteran insects. In T. molitor, most COEs showed tissue and stagespecific but not a sex-biased expression. Our results provide insights into the diversity and evolutionary characteristics of COEs in tenebrionids, and lay a foundation for the functional characterization of COEs in the yellow mealworm.

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Section: Resultsmentioning

confidence: 99%

Comparative genomic analysis of carboxylesterase genes in Tenebrio molitor and other four tenebrionids

Yang

Wang

et al. 2022

Arch Insect Biochem Physiol

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“…lepida transcriptome. Carboxylesterase-6 is the significant allergen in hymenopteran insects’ venoms [ 59 , 65 , 66 , 67 ]. They also have roles as an odorant degrading enzyme in the insect olfactory sensilla [ 68 ].…”

Section: Discussionmentioning

confidence: 99%

Identification of Novel Toxin Genes from the Stinging Nettle Caterpillar Parasa lepida (Cramer, 1799): Insights into the Evolution of Lepidoptera Toxins

Mitpuangchon

Nualcharoen

Boonrotpong

et al. 2021

Insects

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Many animal species can produce venom for defense, predation, and competition. The venom usually contains diverse peptide and protein toxins, including neurotoxins, proteolytic enzymes, protease inhibitors, and allergens. Some drugs for cancer, neurological disorders, and analgesics were developed based on animal toxin structures and functions. Several caterpillar species possess venoms that cause varying effects on humans both locally and systemically. However, toxins from only a few species have been investigated, limiting the full understanding of the Lepidoptera toxin diversity and evolution. We used the RNA-seq technique to identify toxin genes from the stinging nettle caterpillar, Parasa lepida (Cramer, 1799). We constructed a transcriptome from caterpillar urticating hairs and reported 34,968 unique transcripts. Using our toxin gene annotation pipeline, we identified 168 candidate toxin genes, including protease inhibitors, proteolytic enzymes, and allergens. The 21 P. lepida novel Knottin-like peptides, which do not show sequence similarity to any known peptide, have predicted 3D structures similar to tarantula, scorpion, and cone snail neurotoxins. We highlighted the importance of convergent evolution in the Lepidoptera toxin evolution and the possible mechanisms. This study opens a new path to understanding the hidden diversity of Lepidoptera toxins, which could be a fruitful source for developing new drugs.

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“…Wasp venom may result in anaphylaxis, anaphylactic shock, or even death [ 145 , 146 ]. Compared to airborne allergens such as mites and pollen [ 147 ], wasp venom is injected into the skin, reaching the blood directly, and initiating a general immune response [ 145 ].…”

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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Biopanning of allergens from wasp sting patients

Cited by 8 publications

References 42 publications

Comparative genomic analysis of carboxylesterase genes in Tenebrio molitor and other four tenebrionids

Comparative genomic analysis of carboxylesterase genes in Tenebrio molitor and other four tenebrionids

Identification of Novel Toxin Genes from the Stinging Nettle Caterpillar Parasa lepida (Cramer, 1799): Insights into the Evolution of Lepidoptera Toxins

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

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