Thioredoxin from the Indianmeal Moth Plodia interpunctella: Cloning and Test of the Allergenic Potential in Mice

被引:13
|
作者
Hoflehner, Elisabeth [1 ]
Binder, Marina [1 ]
Hemmer, Wolfgang [2 ]
Mahler, Vera [3 ]
Panzani, Raphael C. [4 ]
Jarisch, Reinhart [2 ]
Wiedermann, Ursula [1 ]
Duchene, Michael [1 ]
机构
[1] Med Univ Vienna, Ctr Pathophysiol Infectiol & Immunol, Inst Specif Prophylaxis & Trop Med, Vienna, Austria
[2] Floridsdorfer Allergiezentrum, Vienna, Austria
[3] Univ Erlangen Nurnberg, Dept Dermatol, Erlangen, Germany
[4] Ctr Rech Allergol, Marseille, France
来源
PLOS ONE | 2012年 / 7卷 / 07期
关键词
HOUSE-DUST; CROSS-REACTIVITY; ARGININE KINASE; IGE ANTIBODIES; BAKERS ASTHMA; PAN-ALLERGEN; FAMILY; INSECTS; WHEAT; RESPONSES;
D O I
10.1371/journal.pone.0042026
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Background/Objective: The Indianmeal moth Plodia interpunctella is a highly prevalent food pest in human dwellings, and has been shown to contain a number of allergens. So far, only one of these, the arginine kinase (Plo i 1) has been identified. Objective: The aim of this study was to identify further allergens and characterise these in comparison to Plo i 1. Method: A cDNA library from whole adult P. interpunctella was screened with the serum of a patient with indoor allergy and IgE to moths, and thioredoxin was identified as an IgE-binding protein. Recombinant thioredoxin was generated in E. coli, and tested together with Plo i 1 and whole moth extracts in IgE immunoblots against a large panel of indoor allergic patients' sera. BALB/c mice were immunised with recombinant thioredoxin and Plo i 1, and antibody production, mediator release from RBL cells, T-cell proliferation and cytokine production were measured. Result: For the first time a thioredoxin from an animal species was identified as allergen. About 8% of the sera from patients with IgE against moth extracts reacted with recombinant P. interpunctella thioredoxin, compared to 25% reacting with recombinant Plo i 1. In immunised BALB/c mice, the recombinant allergens both induced classical Th2-biased immune responses such as induction IgE and IgG1 antibodies, upregulation of IL-5 and IL-4 and basophil degranulation. Conclusion: Thioredoxin from moths like Plo i 1 acts like a classical Type I allergen as do the thioredoxins from wheat or corn. This clearly supports the pan-allergen nature of thioredoxin. The designation Plo i 2 is suggested for the new P. interpunctella allergen.
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