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.

Proteomics and Immunological Analysis of a Novel Shrimp Allergen, Pen m 2

“…Arginine kinase has been described as an allergen in the moth (Plodia interpunctella), and recombinant Plo i 1 (the moth arginine kinase) is recognized by sera from 25% of moth-sensitized patients (45). The deduced (lanes 2 and 7), crab (S. serrata) (lanes 3 and 8), lobster (H. gammarus) (lanes 4 and 9), and crawfish (M. thomsoni) (lanes 5 and 10) were probed with polyclonal rabbit anti-Pen m 2 Ab (lanes 1-5) or pooled sera from allergic patients (lanes 6 -10).…”

Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn)

“…Also, arginine kinase has been described as a cross-reacting allergen among crustaceans and between crustaceans and insects [22] . In addition, a myosin light chain (MLC), Lit v 3, and sarcoplasmic calcium-binding protein (SCP), Lit v 4.0101, with molecular weight of 20 kDa and 22 kDa, respectively, were recently demonstrated to be new prawn allergens [23,24] .…”

Assessing the Proteomic Activity of the Venom of the AntEctatomma tuberculatum(Hymenoptera: Formicidae: Ectatomminae)

“…It was found in the venom of solitary wasps Eumenidae Eumenes pomiformis and Orancistrocerus drewseni [34], in the venom of social wasps Polybia paulista (Vespidae), with evidence of its allergenic action in humans [35] as well as in various other invertebrates such as Dermatophagoides pteronyssinus (Acari: Pyroglyphidae), Blatella germanica (Insecta: Blattodea: Blattellidae), Penaeus monodon (Crustacea: Penaeidae), Homarus gammarus (Crustacea: Nephropidae), Mytilus edulis (Mollusca: Bivalvia: Mytilidae), and Plodia interpunctella (Insecta: Lepidoptera: Pyralidae), a new class of allergens [36]. Yamamoto and collaborators [37] have isolated arginine kinase from the venom of solitary wasp Pompilidae Cyphononyx dorsalis and confirmed its paralytic activity in spiders, their natural prey.…”