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Updated: Jan 31, 2026

A Streamlined Approach for Mass Spectrometry-Based Proteomics Using Selected Tissue Regions
Published on: April 18, 2025
Mining allergens in Cryptotympana atrata nymphs: integrating proteomics and homology-based bioinformatics
Yuan He1, Shu-Tao Sun2, Jian-Bo Xiao3
1School of Public Health, Shandong Second Medical University, Weifang, Shandong 261053, PR China; Key Laboratory of Novel Food Resources Processing, Ministry of Agriculture and Rural Affairs/ Institute of Agro-Food Science and Technology, Shandong Academy of Agricultural Sciences, 202 Gongye North Road, Jinan 250100, PR China.
Abstract:
The consumption of novel edible insects carries potential allergenicity risks. Cryptotympana atrata (C. atrata), a common East Asian cicada species, is traditionally consumed in China. Although allergic reactions to C. atrata nymphs have been reported, the specific allergens remain undocumented. The mass spectrometry data of C. atrata nymphs directly detected pan-allergens tropomyosin and arginine kinase. Through comprehensive amino acid sequence alignment and phylogenetic analysis, the evolutionary conservation of these allergens was investigated. The allergens of C. atrata showed high sequence similarity and close phylogenetic relationships to homologous allergens from silkworm and crustaceans. Further 3D modeling and structural alignment demonstrated high similarity between these two C. atrata allergens and their Bombyx mori counterparts. AllerCatPro 2.0 predicted several potential allergens in cicada nymphs, including peroxidase, carboxylesterase, serine carboxypeptidase, filamin, and troponin I. Thus, individuals allergic to silkworm or crustaceans should be cautious of possible cross-reactive allergic reactions when consuming cicada nymphs.
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