title: Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen.
abstract: IgE recognition of indoor allergens represents a major cause of allergic asthma in atopic individuals. We found that 52 of 102 patients suffering from allergic symptoms indoors contained IgE Abs against allergens from the Indianmeal moth (Plodia interpunctella), a ubiquitous food pest. Using serum IgE from a moth-sensitized patient we screened an expression cDNA library constructed from P. interpunctella larvae. cDNAs coding for arginine kinase (EC 2.7.3.3), a 40-kDa enzyme commonly occurring in invertebrates that is involved in the storage of such high-energy phosphate bonds as phosphoarginine, were isolated. Recombinant moth arginine kinase, designated Plo i 1, was expressed in Escherichia coli as a histidine-tagged protein with enzymatic activity, and purified to homogeneity by nickel chelate affinity chromatography. Purified recombinant arginine kinase induced specific basophil histamine release and immediate as well as late-phase skin reactions. It reacted with serum IgE from 13 of the 52 (25%) moth-allergic patients and inhibited the binding of allergic patients' IgE to an immunologically related 40-kDa allergen present in house dust mite, cockroach, king prawn, lobster, and mussel. Our results indicate that arginine kinases represent a new class of cross-reactive invertebrate pan-allergens. Recombinant arginine kinase may be used to identify a group of polysensitized indoor allergic patients and for immunotherapy of these individuals.
authors.affiliation: Division of Specific Prophylaxis and Tropical Medicine and Immunopathology, Department of Pathophysiology, University of Vienna, Vienna, Austria.
authors.forename: M
authors.initials: M
authors.lastname: Binder
authors.forename: V
authors.initials: V
authors.lastname: Mahler
authors.forename: B
authors.initials: B
authors.lastname: Hayek
authors.forename: W R
authors.initials: WR
authors.lastname: Sperr
authors.forename: M
authors.initials: M
authors.lastname: Schöller
authors.forename: S
authors.initials: S
authors.lastname: Prozell
authors.forename: G
authors.initials: G
authors.lastname: Wiedermann
authors.forename: P
authors.initials: P
authors.lastname: Valent
authors.forename: R
authors.initials: R
authors.lastname: Valenta
authors.forename: M
authors.initials: M
authors.lastname: Duchêne
mesh_terms: D000293:Adolescent; D000328:Adult; D000485:Allergens / Q000276:immunology*; D000595:Amino Acid Sequence; D000818:Animals; D001122:Arginine Kinase / Q000737:chemistry / Q000276:immunology* / Q000302:isolation & purification; D001483:Base Sequence; D002648:Child; D003058:Cockroaches / Q000276:immunology; D003429:Cross Reactions; D006636:Histamine Release; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D008875:Middle Aged; D008925:Mites / Q000276:immunology; D008969:Molecular Sequence Data; D009036:Moths / Q000276:immunology*; D011994:Recombinant Proteins / Q000302:isolation & purification
chemical_list: D000485:Allergens; D011994:Recombinant Proteins; D007073:Immunoglobulin E; D001122:Arginine Kinase