| Title : Mining allergens in Cryptotympana atrata nymphs: integrating proteomics and homology-based bioinformatics - He_2026_Food.Chem_506_148144 |
| Author(s) : He Y , Sun ST , Xiao JB , Ren QD , Chen YY , Zhang MQ , Wang MX , Guo X , Sun JY , Liu C |
| Ref : Food Chem , 506 :148144 , 2026 |
|
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. |
| PubMedSearch : He_2026_Food.Chem_506_148144 |
| PubMedID: 41610773 |
He Y, Sun ST, Xiao JB, Ren QD, Chen YY, Zhang MQ, Wang MX, Guo X, Sun JY, Liu C (2026)
Mining allergens in Cryptotympana atrata nymphs: integrating proteomics and homology-based bioinformatics
Food Chem
506 :148144
He Y, Sun ST, Xiao JB, Ren QD, Chen YY, Zhang MQ, Wang MX, Guo X, Sun JY, Liu C (2026)
Food Chem
506 :148144