Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.65 (Der p 1)
 346 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A liquid-phase, antigen-binding radioimmunoassay measuring subclass IgG4 antibody (ab) to allergens has been developed. This assay, which uses monoclonal anti-IgG4 to bind IgG4, allows direct comparison of class (IgG)- and subclass (IgG4)-specific ab levels. These assays used radiolabeled purified allergens, Der p I (Ag P1) from the dust mite Dermatophagoides pteronyssinus, Lol p I (Rye 1), from ryegrass pollen, hen's egg ovalbumin, and beta-lactoglobulin from cow's milk. We have investigated IgG4 abs in several clinical situations. The results confirm that IgG ab responses to both inhalants and food proteins unequivocally include IgG4 ab. On average, the proportion of IgG4 ab to these antigens is far higher than the contribution of IgG4 to total IgG. In patients with adult atopic dermatitis, levels of both class and subclass ab were higher than in control subjects; however, the ratio of IgG4:IgG varied widely in patients and control subjects. During desensitization treatment of patients with perennial rhinitis, levels of IgG4 ab to Der p 1 increased sharply, but there were also increases in the total IgG ab responses so that the percentage contribution of IgG4 was only moderately increased (mean values: before, 29%; after, 36%). In a prospective study of children from atopic families, IgG4 abs to food proteins were detectable as early as 3 months. IgG abs to hen's egg ovalbumin and beta-lactoglobulin from cow's milk increased to a maximum at 3 years and declined by 5 years. However, specific IgG4 as a percentage of specific IgG increased progressively from a mean value of approximately 15% at 6 months to approximately 50% at 5 years of age.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A subclass IgG4-specific antigen-binding radioimmunoassay (RIA): comparison between IgG and IgG4 antibodies to food and inhaled antigens in adult atopic dermatitis after desensitization treatment and during development of antibody responses in children. 366 26

To determine the tolerance of an allergen extract standardized in mass units, we closely monitored the side-effects, during the buildup phase of immunotherapy treatment, in 88 patients with well-documented respiratory allergy to house-dust mite (Dermatophagoides pteronyssinus). Thirty-four patients (38.6%) suffered from moderate perennial rhinitis, and 54 had mild to moderate bronchial asthma (61.4%). For the desensitizing treatment, we used a depot extract adsorbed in aluminum hydroxide of D. pteronyssinus (Pangramin Depot UM), biologically standardized and having the major allergens Der p 1 and Der p 2 quantified in micrograms. A total of 1244 doses were administered. All patients except one (98.9%) reached the expected maximum dose of 4 micrograms Der p 1. Only five patients suffered mild adverse reactions (5.7%). All adverse reactions except one appeared to be related to the vial of maximum concentration: vial III (4 micrograms Der p 1). Considering the number of patients who had adverse reactions and the frequency of adverse reactions per dose, we found no significant differences between rhinitis and asthma sufferers. We think that immunotherapy in doses of 4 micrograms Der p 1 and 2 micrograms Der p 2 is well tolerated and should not be avoided in mildly to moderately asthmatic patients when treating house-dust mite allergy.
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PMID:A prospective safety-monitoring study of immunotherapy in mite-allergy patients with mass-units-standardized extract. 920 72

European (Dermatophagoides pteronyssinus) and American (Dermatophagoides farinae) house dust mite species are considered the most common causes of asthma and allergic symptoms worldwide. Der p 1 protein, one of the main allergens of D. pteronyssinus, is found in high concentration in mites faecal pellets, which can became easily airborne and, when inhaled, can cause perennial rhinitis and bronchial asthma. Here we report the isolation of the Der p 1 gene from an Italian strain of D. pteronyssinus and the PVX-mediated expression of its mature form (I-rDer p 1) in Nicotiana benthamiana plants. Human sera from characterized allergic patients were used for IgE binding inhibition assays to test the immunological reactivity of I-rDer p 1 produced in N. benthamiana plants. The binding properties of in planta produced I-rDer p 1 versus the IgE of patients sera were comparable to those obtained on Der p 1 preparation immobilized on a microarray. In this paper we provide a proof of concept for the production of an immunologically active form of Der p 1 using a plant viral vector. These results pave the way for the development of diagnostic allergy tests based on in planta produced allergens.
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PMID:In planta expression of a mature Der p 1 allergen isolated from an Italian strain of Dermatophagoides pteronyssinus. 2190 13