Baculoviral infection reduces the expression of four allergen proteins of silkworm pupa

• Published in: Archives of insect biochemistry and physiology Vol. 100; no. 4; pp. e21539 - n/a
• Main Authors: Ling, Xiao‐Dong, Dong, Wei‐Tao, Zhang, Yong, Hu, Jun‐Jie, Zhang, Wang‐Dong, Wu, Jin‐Tang, Liu, Ji‐Xing, Zhao, Xing‐Xu
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.04.2019
• Subjects: allergen; Allergens; Allergic diseases; Allergic reactions; Allergies; Antibodies; Arginine; Arginine kinase; Baculovirus; baculovirus vector; bioreactor; Bombyx mori; Dental materials; Drug delivery; Drug delivery systems; Expression vectors; Gene expression; Glycoproteins; Hypersensitivity; Immunological tolerance; Infections; Insect cells; Insects; Larvae; Peroxiredoxin; Polyclonal antibodies; Protein expression; Proteins; Proteomics; Pupae; Ribonucleic acid; RNA; silkworm pupa; Silkworms; baculovirus vector; silkworm pupa; allergen; bioreactor
• ISSN: 0739-4462; 1520-6327
• DOI: 10.1002/arch.21539

Silkworm (Bombyx mori) larvae are widely used to express exogenous proteins. Moreover, some silkworm pupal proteins can be used as drug‐loading materials for selfexpressed oral tolerance drugs. However, several proteins expressed in silkworm pupae cause severe allergic reactions in humans and animals. Interestingly, some baculovirus vectors have been shown to alter the host gene and its expression in insect cells, but this has not been confirmed in silkworm. Here, we analyzed the effects of infection with an empty B. mori baculovirus (BmNPV) vector on silkworm pupal protein expression. Using a proteomics approach, the allergens thiol peroxiredoxin (Jafrac1), 27‐kDa glycoprotein (p27k), arginine kinase, and paramyosin as well as 32 additional differentially expressed proteins were identified. Downregulation of the messenger RNA expression of the four known allergens was observed after BmNPV infection; subsequent changes in protein expression were confirmed by the western blot analysis using polyclonal antibodies prepared with recombinant proteins of the four allergens. Collectively, these data indicate that the four known allergens of silkworm pupae can be reduced by infection ith an empty BmNPV vector to increase the safety of silkworm pupa‐based exogenous protein expression and drug delivery of oral pharmaceuticals. In addition, the four recombinant allergen proteins may contribute to the diagnosis of allergic diseases of silkworm pupa. The peculiar physiological and pharmacological activities of silkworm pupa proteins make them excellent carriers for oral tolerance drugs. However, a variety of silkworm pupa proteins can cause allergic reactions in humans and animals, which limits their application in clinical practice. This study demonstrated, for the first time, that empty BmNPV vectors can reduce the expression of four important allergen proteins in silkworm pupae. The results obtained provide a theoretical basis for the safety of using silkworm pupa proteins as a clinical drug delivery system.