title: Thioredoxin from the Indianmeal moth Plodia interpunctella: cloning and test of the allergenic potential in mice.
abstract: 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.
  
  
  METHODS
  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.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  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.
authors: Institute of Specific Prophylaxis and Tropical Medicine, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Austria.
authors: Elisabeth
authors: E
authors: Hoflehner
authors: Marina
authors: M
authors: Binder
authors: Wolfgang
authors: W
authors: Hemmer
authors: Vera
authors: V
authors: Mahler
authors: Raphael C
authors: RC
authors: Panzani
authors: Reinhart
authors: R
authors: Jarisch
authors: Ursula
authors: U
authors: Wiedermann
authors: Michael
authors: M
authors: Duchêne
mesh_terms: D000293:Adolescent; D000328:Adult; D000368:Aged; D000485:Allergens / Q000737:chemistry / Q000235:genetics* / Q000276:immunology*; D000595:Amino Acid Sequence; D000818:Animals; D001122:Arginine Kinase / Q000276:immunology; D002648:Child; D002675:Child, Preschool; D003001:Cloning, Molecular; D016207:Cytokines / Q000096:biosynthesis; D005260:Female; D006801:Humans; D006967:Hypersensitivity / Q000097:blood / Q000378:metabolism; D007114:Immunization; D007073:Immunoglobulin E / Q000096:biosynthesis / Q000097:blood / Q000276:immunology; D007223:Infant; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics* / Q000276:immunology*; D007915:Lepidoptera / Q000235:genetics* / Q000276:immunology; D008297:Male; D051379:Mice; D008875:Middle Aged; D008969:Molecular Sequence Data; D013879:Thioredoxins / Q000737:chemistry / Q000235:genetics* / Q000276:immunology*; D055815:Young Adult
chemical_list: D000485:Allergens; D016207:Cytokines; D019476:Insect Proteins; D007073:Immunoglobulin E; D013879:Thioredoxins; D001122:Arginine Kinase