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BackgroundAllergen immunotherapy is a treatment modality which can be applied using different vaccines. The aim of this study was to quantify and compare the allergen content of different house dust mites (HDM)’ sublingual treatments and to review the evidence on their efficacy.MethodsFive sublingual allergen immunotherapy (SLIT) products were ordered and purchased at an ordinary pharmacy and masked for blinding before the study was started. Detection of Dermatophagoides pteronyssinus and Dermatophagoides farinae allergens Der p 1, Der f 1, Der p 2 and Der f 2 was carried out by immunoblotting and fluorescent multiplex. A literature search for meta‐analyses and systematic reviews that included SLIT‐HDM products was performed.ResultsDer p 1 concentrations ranged from 0.6 to 14.5 μg/ml; similar figures were found for Der f 1 that ranged from 0.2 to 12.4 μg/ml. Der p 2+ Der f 2 ranged from 0.2 to 1.5 μg/ml. Data on efficacy are scarce for most of the five products.ConclusionsSubstantial variations regarding allergen content were found among these five SLIT‐HDM products. Therefore, it can be necessary to guarantee the quality of the SLIT‐HDM products and to demonstrate their effectiveness before they are marketed. It seems necessary, for the moment, to take into account these characteristics of the products before prescribing.

Background:Salsola kali is an Amaranthaceae weed with important repercussions for pollinosis in temperate areas. Ole e 1-like members are relevant allergens in pollen from different species. We aimed to characterize and produce as recombinant allergen S. kali Ole e 1-like protein. Methods: The natural allergen was purified at homogeneity after three chromatographic steps. Specific cDNA was sequenced and expressed in Pichia pastoris yeast. Structural relationships of natural and recombinant forms were carried out by 2D electrophoresis and spectroscopic analyses. Its immunological relevance was analyzed by ELISA and immunoblotting using an IgG antiserum and monoclonal antibodies specific to Ole e 1, as well as sera from 57 allergic patients recruited from two Spanish regions where this pollinosis is frequent. Results: The purified allergen, Sal k 5, is an acidic glycoprotein of 151 amino acid residues and 17,628 Da of molecular mass. Its amino acid sequence exhibits 68 and 32% identity with the allergens of Che a 1 and Ole e 1, respectively. The recombinant protein was correctly processed and its structural and immunologic equivalence to the natural form was proven. A sensitization frequency between 30 and 40% was observed in pollinic patients from the center and east coast of Spain. Conclusions: Sal k 5 is a member of the Ole e 1-like protein family which can be considered an important allergen from S. kali. Its inclusion in diagnosis protocols would allow the accurate defining of patients allergic to this pollen.