PurposeThe clinical efficacy of allergen-immunotherapy is known to be dose dependent. However, optimal maintenance dosage has not yet been determined for sublingual immunotherapy (SLIT). Furthermore, since companies adopt their own units for expression of allergenicity, the allergen concentrations of individual reagents cannot be compared easily. We sought to measure and compare the allergenicities of 3 commercially available house dust mite (HDM) SLIT regents and a subcutaneous immunotherapy reagent.MethodsWe measured the HDM allergenic potency of the maintenance dosages of three SLIT reagents: Staloral® (300 index of reactivity [IR] /mL, recommended maintenance dosage [MD]: 120 IR), SLITone® (1,000 standard therapeutic unit [STU]/mL, recommended MD: 200 STU), Wolwopharma® (100 µg/mL, recommended MD: 20 µg), and subcutaneous immunotherapy regents of Hollister-Stier (10,000 allergy unit [AU] /mL). The allergenic potency was assessed by measuring the total protein concentrations, mite group 1 and 2 allergens using 2-site ELISA, and an inhibition test against IgE specific to Dermatophagoides farinae and Dermatophagoides pteronyssinus.ResultsThe protein content of the Wolwopharma® reagent was 1.5-261.4 times higher than that of the other 2 SLIT reagents. The concentration of group 1 major allergens in Staloral® (132.03 µg/mL) was 33- to 44.5-fold higher than in SLITone® (4.00 µg/mL) and Wolwopharma® (2.97 µg/mL). The concentration of group 2 major allergen was also 8.9- to 10.5-fold higher in Staloral® (15.7 µg/mL) than in SLITone® (1.8 µg/mL) or Wolwopharma® (1.5 µg/mL). An ELISA inhibition study against HDM-specific IgE showed that the allergen potency of Staloral® reagent is 8.5-fold and 21-fold higher than that of SLITone® or Wolwopharma®, respectively. The differences between the maintenance dosages are further exaggerated by the differences in the recommended volumes of SLIT reagents.ConclusionsThe allergen potencies of commercially available HDM SLIT reagents are markedly different. Consensus regarding the optimal allergen concentration for SLIT reagents used to treat HDM respiratory allergies is needed.

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The first gene encoding gamma-glutamyl transpeptidase (GGTI) of the fission yeast has previously been characterized, and its expression was found to be regulated by various oxidative stress-inducing agents. In this work, a second gene, encoding GGTII, was cloned and characterized from the fission yeast Schizosaccharomyces pombe. The structural gene encoding GGTII was amplified from the genomic DNA of the fission yeast and ligated into the shuttle vector pRS316 to generate the recombinant plasmid pPHJ02. The determined sequence contains 3040 bp and is able to encode the putative 611 amino acid sequence of GGTII, which resembles the counterparts of Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus, and Escherichia coli. The DNA sequence also contains 940-bp upstream and 289-bp downstream regions of the GGTII gene. The Schizosaccharomyces pombe cells harboring plasmid pPHJ02 showed about 4-fold higher GGT activity in the exponential phase than the cells harboring the vector only, indicating that the cloned GGTII gene is functional. The S. pombe cells containing the cloned GGTII gene were found to contain higher levels of both intracellular glutathione (GSH) content and GSH uptake. The S. pombe cells harboring plasmid pPHJ02 showed increased survival on solid media containing hydrogen peroxide, diethylmaleate, aluminum chloride, cadmium chloride, or mercuric chloride. The GGTII mRNA level was significantly elevated by treatment with GSH-depleting diethylmaleate. These results imply that the S. pombe GGTII gene produces functional GGTII protein and is involved in the response to oxidative stresses in S. pombe cells.