Allergenic Activity of Individual Cat Allergen Molecules.

More than 10% of the world's population suffers from an immunoglobulin E (IgE)-mediated allergy to cats which is accompanied mainly by respiratory symptoms such as rhinitis and asthma. Several cat allergen molecules have been identified, but their allergenic activity has not been investigated in depth. Purified cat allergen molecules (Fel d 1, Fel d 2, Fel d 3, Fel d 4, Fel d 6, Fel d 7 and Fel d 8) were characterized via mass spectrometry and circular dichroism spectroscopy regarding their molecular mass and fold, respectively. Cat-allergen-specific IgE levels were quantified via ImmunoCAP measurements in IgE-sensitized subjects with (n = 37) and without (n = 20) respiratory symptoms related to cat exposure. The allergenic activity of the cat allergens was investigated by loading patients' IgE onto rat basophils expressing the human FcεRI receptor and studying the ability of different allergen concentrations to induce ß-hexosaminidase release. Purified and folded cat allergens with correct masses were obtained. Cat-allergen-specific IgE levels were much higher in patients with a respiratory allergy than in patients without a respiratory allergy. Fel d 1, Fel d 2, Fel d 4 and Fel d 7 bound the highest levels of specific IgE and already-induced basophil degranulation at hundred-fold-lower concentrations than the other allergens. Fel d 1, Fel d 4 and Fel d 7 were recognized by more than 65% of patients with a respiratory allergy, whereas Fel d 2 was recognized by only 30%. Therefore, in addition to the major cat allergen Fel d 1, Fel d 4 and Fel d 7 should also be considered to be important allergens for the diagnosis and specific immunotherapy of cat allergy.

Albumins represent highly cross-reactive animal allergens.

Albumins from animals are highly cross-reactive allergens for patients suffering from immunoglobulin E (IgE)-mediated allergy. Approximately 20-30% of cat and dog allergic patients show IgE reactivity and mount IgE-mediated allergic reactions to cat and dog albumin. It is astonishing that allergic patients can develop specific IgE responses against animal albumins because these proteins exhibit a more than 70% sequence identity to human serum albumin (HSA) which is the most abundant protein in the blood of the human body. The sequence identity of cat albumin (Fel d 2) and dog albumin (Can f 3) and HSA are 82% and 80%, respectively. Given the high degree of sequence identity between the latter two allergens and HSA one would expect that immunological tolerance would prohibit IgE sensitization to Fel d 2 and Can f 3. Here we discuss two possibilities for how IgE sensitization to Fel d 2 and Can f 3 may develop. One possibility is the failed development of immune tolerance in albumin-allergic patients whereas the other possibility is highly selective immune tolerance to HSA but not to Fel d 2 and Can f 3. If the first assumption is correct it should be possible to detect HSA-specific T cell responses and HSA-containing immune complexes in sensitized patients. In the latter scenario few differences in the sequences of Fel d 2 and Can f 3 as compared to HSA would be responsible for the development of selective T cell and B cell responses towards Fel d 2 as well as Can f 3. However, the immunological mechanisms of albumin sensitization have not yet been investigated in detail although this will be important for the development of allergen-specific prevention and allergen-specific immunotherapy (AIT) strategies for allergy to albumin.

Milk Allergen Micro-Array (MAMA) for Refined Detection of Cow's-Milk-Specific IgE Sensitization.

BACKGROUND: Immunoglobulin-E(IgE)-mediated hypersensitivity to cow's milk allergens is a frequent cause of severe and life-threatening anaphylactic reactions. Besides case histories and controlled food challenges, the detection of the IgE antibodies specific to cow's milk allergens is important for the diagnosis of cow-milk-specific IgE sensitization. Cow´s milk allergen molecules provide useful information for the refined detection of cow-milk-specific IgE sensitization. METHODS: A micro-array based on ImmunoCAP ISAC technology was developed and designated milk allergen micro-array (MAMA), containing a complete panel of purified natural and recombinant cow's milk allergens (caseins, α-lactalbumin, ß-lactoglobulin, bovine serum albumin-BSA and lactoferrin), recombinant BSA fragments, and α-casein-, α-lactalbumin- and ß-lactoglobulin-derived synthetic peptides. Sera from 80 children with confirmed symptoms related to cow's milk intake (without anaphylaxis: n = 39; anaphylaxis with a Sampson grade of 1-3: n = 21; and anaphylaxis with a Sampson grade of 4-5: n = 20) were studied. The alterations in the specific IgE levels were analyzed in a subgroup of eleven patients, i.e., five who did not and six who did acquire natural tolerance. RESULTS: The use of MAMA allowed a component-resolved diagnosis of IgE sensitization in each of the children suffering from cow's-milk-related anaphylaxis according to Sampson grades 1-5 requiring only 20-30 microliters of serum. IgE sensitization to caseins and casein-derived peptides was found in each of the children with Sampson grades of 4-5. Among the grade 1-3 patients, nine patients showed negative reactivity to caseins but showed IgE reactivity to alpha-lactalbumin (n = 7) or beta-lactoglobulin (n = 2). For certain children, an IgE sensitization to cryptic peptide epitopes without detectable allergen-specific IgE was found. Twenty-four children with cow-milk-specific anaphylaxis showed additional IgE sensitizations to BSA, but they were all sensitized to either caseins, alpha-lactalbumin, or beta-lactoglobulin. A total of 17 of the 39 children without anaphylaxis lacked specific IgE reactivity to any of the tested components. The children developing tolerance showed a reduction in allergen and/or peptide-specific IgE levels, whereas those remaining sensitive did not. CONCLUSIONS: The use of MAMA allows for the detection, using only a few microliters of serum, of IgE sensitization to multiple cow's milk allergens and allergen-derived peptides in cow-milk-allergic children with cow-milk-related anaphylaxis.

Use of an antiseptic rinse (NanArgol) for the oral hygiene maintenance of subjects with fixed appliances: A randomized clinical trial.

BACKGROUND: The risk of periodontal diseases development increased in patients with malocclusion undergoing orthodontic treatment. Thus, the aim of this study was to examine the efficacy of the use of adjunctive rinses with nano-Argentum to standard oral hygiene regimen in subjects wearing fixed orthodontic appliances. MATERIALS AND METHODS: Eighty patients were observed for 1 year. They were divided in two groups: in test group patients were instructed to rinse with non-ionic colloidal silver solution according to protocol for 6 months as an adjunct to standard; in control group the patients followed the standard oral hygiene regimen. Index of efficiency of oral hygiene (PHPm), community periodontal index (CPI) and papillary-marginal-alveolar index (PMA) were evaluated before treatment and after 1 and 6 months. For statistics analysis, Mann-Whitney, Kruskal-Wallis tests and Pearson criterion were used. RESULTS: Baseline hygiene levels in two groups had no differences. Oral hygiene indices were significantly lower in the test group in comparison with control after 1 month (PHPm = 0.38 ± 0.18 and 1.19 ± 0.45, respectively, p < 0.01; PMA = 11.78 ± 8.5 and 47.25 ± 20.9, respectively, p < 0.05; CPI = 0.65 ± 0.53 and 1.53 ± 0.77, respectively, p < 0.01) and 6 months (PHPm = 0.5 ± 0.2 and 1.2 ± 0.4, respectively, p < 0.01; PMA = 11.62 ± 19.6 and 66.33 ± 27.9, respectively, p < 0.01; CPI = 0.63 ± 0.73 and 1.68 ± 0.78, respectively, p < 0.01). CONCLUSIONS: The use of the test solution as an adjunct to standard oral hygiene provided a significant beneficial effect in terms of oral hygiene in patients undergoing orthodontic treatment.

Vitamin D and Its Role in Oral Diseases Development. Scoping Review.

Vitamin D is a fat-soluble secosteroid that plays a significant role in the whole body, including the maxillofacial region. The discovery of its receptors in many cells and organs made it possible to reveal the participation of vitamin D not only in the regulation of calcium phosphate metabolism, but also in immune processes, in providing anti-inflammatory and antimicrobial effects, slowing down cell proliferation and stimulating differentiation. In this literature review, we demonstrate the association between low vitamin D levels and the development of recurrent aphthous stomatitis, the course and response to treatment of squamous cell carcinoma of the oral cavity, the severity of periodontal diseases, and the processes of osseointegration and bone remodeling during dental implantation and guided tissue regeneration. The aim of our article was to demonstate a possible connection between vitamin D level and the oral diseases that can be presented at an oral surgery appointment, which will help clinicians to reduce the risk of early dental implant failure, ensure favorable outcomes of augmentative operations, as well as decrease the destructive effects of severe periodontitis and other conditions throug knowledge and timely lab tests and endocrinologist prescriptions.

The allergenic activity and clinical impact of individual IgE-antibody binding molecules from indoor allergen sources.

A large number of allergens have been discovered but we know little about their potential to induce inflammation (allergenic activity) and symptoms. Nowadays, the clinical importance of allergens is determined by the frequency and intensity of their IgE antibody binding (allergenicity). This is a rather limited parameter considering the development of experimental allergology in the last 20 years and the criteria that support personalized medicine. Now it is known that some allergens, in addition to their IgE antibody binding properties, can induce inflammation through non IgE mediated pathways, which can increase their allergenic activity. There are several ways to evaluate the allergenic activity, among them the provocation tests, the demonstration of non-IgE mediated pathways of inflammation, case control studies of IgE-binding frequencies, and animal models of respiratory allergy. In this review we have explored the current status of basic and clinical research on allergenic activity of indoor allergens and confirm that, for most of them, this important property has not been investigated. However, during recent years important advances have been made in the field, and we conclude that for at least the following, allergenic activity has been demonstrated: Der p 1, Der p 2, Der p 5 and Blo t 5 from HDMs; Per a 10 from P. americana; Asp f 1, Asp f 2, Asp f 3, Asp f 4 and Asp f 6 from A. fumigatus; Mala s 8 and Mala s 13 from M. sympodialis; Alt a 1 from A. alternata; Pen c 13 from P. chrysogenum; Fel d 1 from cats; Can f 1, Can f 2, Can f 3, Can f 4 and Can f 5 from dogs; Mus m 1 from mice and Bos d 2 from cows. Defining the allergenic activity of other indoor IgE antibody binding molecules is necessary for a precision-medicine-oriented management of allergic diseases.