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        <title>Frontiers in Allergy | Allergens section | New and Recent Articles</title>
        <link>https://www.frontiersin.org/journals/allergy/sections/allergens</link>
        <description>RSS Feed for Allergens section in the Frontiers in Allergy journal | New and Recent Articles</description>
        <language>en-us</language>
        <generator>Frontiers Feed Generator,version:1</generator>
        <pubDate>2026-05-13T08:50:35.458+00:00</pubDate>
        <ttl>60</ttl>
        <item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2026.1816013</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2026.1816013</link>
        <title><![CDATA[Two combinations of house dust mite allergens show similar performance than extracts for asthma diagnosis]]></title>
        <pubdate>2026-04-10T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Victoria Marrugo</author><author>Josefina Zakzuk</author><author>Randy Reina</author><author>Karen Donado</author><author>Ronald Regino</author><author>Isabel Gil</author><author>Caterine Meza</author><author>Dilia Mercado</author><author>Enrique Fernández-Caldas</author><author>Leonardo Puerta</author><author>Nathalie Acevedo</author><author>Luis Caraballo</author>
        <description><![CDATA[IntroductionMolecular allergy diagnostics for house dust mite (HDM) sensitization includes both allergenic molecules and extracts, but extracts have batch-to-batch variability, incomplete allergen representation and cross-reactivity, which confound results and reduces test accuracy. However, although using extract-free arrays could solve these problems, there is no study that formally supports this change. Therefore, the aim of this study was to compare the diagnostic performance and clinical relevance of measuring specific IgE to Dermatophagoides pteronyssinus and Blomia tropicalis extracts vs. two allergen combinations, Blo t 2/Blo t 5/Blo t 21 and Der p 1/Der p 2/Der p 23.MethodsIn 201 adults with asthma and matched controls, diagnostic performance of specific IgE towards molecular allergen combinations and extracts were compared using receiver operator characteristics analysis, with physician-diagnosed asthma as reference standard. Associations between specific IgE (extracts and combinations) and type 2 inflammation biomarkers (fractional exhaled nitric oxide and blood eosinophils) were also evaluated.ResultsSpecific IgE frequencies and levels were higher in patients. Allergen combinations and extracts showed equivalent performance. The area under the curve of the combination Blo t 2/Blo t 5/Blo t 21 was similar to that of the B. tropicalis extract: 0.783 and 0.808 respectively (p = 0.42). Likewise, the area under the curve of the combination Der p 1/Der p 2/Der p 23 was 0.793 and that of extract was 0.788 (p = 0.8). Notably, IgE response to D. pteronyssinus allergens was more specific than the extract and significantly associated with fractional exhaled nitric oxide and blood eosinophils.ConclusionOur findings provide, for the first time, direct evidence that specific allergen combinations have similar diagnostic performance to HDM extracts in molecular diagnostics, improving test accuracy and supporting a shift toward standardized, molecular-resolved diagnostic strategies. In addition, we found that allergen combinations, and not HDM extracts, are strongly associated with type 2 inflammation biomarkers, supporting their use for personalized asthma management.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2026.1842963</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2026.1842963</link>
        <title><![CDATA[Retraction: Mechanisms for Alternaria alternata function in the skin during induction of peanut allergy in neonatal mice with skin barrier mutations]]></title>
        <pubdate>2026-04-02T00:00:00Z</pubdate>
        <category>Retraction</category>
        
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2025.1663395</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2025.1663395</link>
        <title><![CDATA[Case Report: Severe IgE-mediated hypersensitivity to carboxymethylcellulose with tolerance to crosscarmellose and microcrystalline cellulose]]></title>
        <pubdate>2025-10-24T00:00:00Z</pubdate>
        <category>Case Report</category>
        <author>Rhea Schreiber</author><author>Carole Guillet</author>
        <description><![CDATA[We present a rare case of severe IgE-mediated hypersensitivity to carboxymethylcellulose (CMC) following an intraarticular knee injection with triamcinolone acetonide (Triamcort®). The patient experienced a grade IV anaphylactic reaction shortly after administration. Diagnostic workup, including skin prick testing and basophil activation test, confirmed sensitization to CMC. Importantly, the patient tolerated medications containing crosscarmellose and microcrystalline cellulose without adverse reactions, suggesting no clinically relevant cross-reactivity. This case highlights the need to consider excipients such as CMC as potential triggers of severe allergic reactions especially in cases of unexplained anaphylaxis to injectable medication and underscores the importance of thorough allergological assessment to ensure safe future treatments.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2025.1616730</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2025.1616730</link>
        <title><![CDATA[Sensitization to inhaled and food allergen sources in patients with allergic diseases in Eastern China]]></title>
        <pubdate>2025-08-20T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Zhibang Hu</author><author>Chunhui Wang</author><author>Jianrong Xue</author><author>Shiyu Yang</author><author>Yongzheng Bao</author><author>Yunhui Wu</author><author>Xiaoju Hou</author><author>Yishake Kaiseer</author><author>Jing Ma</author>
        <description><![CDATA[BackgroundAllergen exposure plays a critical role in the onset of allergic disease, and the distribution of allergens varies by geographic location, climate, and lifestyle.MethodsA retrospective analysis was conducted on the data of 4,149 patients with clinically suspected allergic diseases who sought medical care at Changzhou Third People's Hospital. The total IgE and specific IgE (sIgE) levels for 19 inhaled and food allergen sources were assessed using the Mediwiss AllergyScreen system. The sensitization patterns to various allergen sources were delineated based on sex and age categories.ResultsA total of 2,491 (60.04%) patients were positive for sIgE to at least one allergen source. Specifically, 997 (40.02%) patients were positive for one allergen source, while 1,494 (59.98%) were positive for two or more allergen sources. The sensitization rate for inhaled allergen sources was 49.41% (2,050), which was significantly higher than that for food allergen sources at 36.61% (1,519) (p < 0.05). The most commonly inhaled allergen source was D. pteronyssinus (37.58%, 1,559/4,149), followed by mold mix (13.11%, 544/4,149) and house dust (9.11%, 378/4,149). Among food allergen sources, the most prevalent reactions were cashew nut (15.57%, 646/4,149), cow's milk (10.99%, 456/4,149), and egg (9.33%, 387/4,149). The majority of sIgE levels were concentrated in the lower grades (grade I to III), while eight cases of crab and six cases of shrimp allergen sources presented at the highest responses (grade IV). Males exhibited significantly higher sIgE-positive rates for both inhaled and food allergen sources than females (p < 0.05). Additionally, the sIgE-positive rates for most inhaled and food allergen sources displayed significant variations across different age groups (p < 0.05). The highest sIgE-positive rate for inhaled allergen sources was observed in the 11–15 years group, and the positive rates of sIgE for food allergen sources decreased with advancing age. The levels of total serum IgE also varied among different age groups, with 2,631 (63.41%) individuals belonging to the high-concentration group. Total serum IgE exhibited an upward trend until the age of 11–15 years, which was then followed by a steady decrease.ConclusionThe results revealed the sensitization characteristics of allergen sources in eastern China, providing valuable insights into the prevention, diagnosis, and management of allergic diseases in this region.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2025.1605074</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2025.1605074</link>
        <title><![CDATA[Allergic rhinitis in college students at Dongguan: a cross-sectional survey on disease burden, knowledge, and self-management]]></title>
        <pubdate>2025-06-17T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Xin Peng</author><author>Haiyi Yan</author><author>Haixin Feng</author><author>Shiqing Huang</author><author>Bingsong Zhang</author><author>Xueqin Huang</author>
        <description><![CDATA[This study examined the prevalence, clinical characteristics, disease knowledge, and quality of life impact of allergic rhinitis (AR) among college students in Dongguan, China. Using a customized questionnaire, we surveyed 1,531 participants (response rate: 85.1%) and identified an AR prevalence of 18.68% (95% CI: 16.72–20.63%). The study identified significant gaps in AR management, including underutilization of allergen testing (only 44.21% of AR patients underwent skin prick testing) and limited medication knowledge among 73% of participants. Environmental control measures were often neglected, and health education was inconsistently delivered, with 72.03% of students relying on the internet for AR information. The findings underscore the need for enhanced health education, improved access to diagnostic testing, and patient-centered communication strategies. Digital platforms and peer-led interventions are recommended to address these gaps and improve AR self-management.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1478392</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1478392</link>
        <title><![CDATA[Common pollen and related allergen components in patients with allergic diseases in the Beijing area]]></title>
        <pubdate>2024-11-21T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Yi-Bo Hou</author><author>Jin-Lu Sun</author>
        <description><![CDATA[BackgroundPollen is the most common outdoor allergen that causes allergic rhinitis and asthma, which seriously affects patient quality of life and extensive cross-reactivity occurs between pollen allergens.MethodsThe study enrolled 84 patients with respiratory allergies and at least one pollen allergy who visited the clinic. Specific-IgE was detected via immunoblotting in the sera of patients with positive respiratory allergies to pollen. IgE of the components and cross-reactive carbohydrate determinants (CCD) were evaluated using a fluorescence-encoded microsphere assay.ResultsOur results suggest that Artemisia absinthium, Artemisia vulgaris, Humulus scandens, Amaranthus, Parietaria micrantha allergies are most common in the northern region, and that weed pollen remains the major pollen allergen in the northern region. Among the different age groups, the positive rate of Platanus pollen allergens was significantly higher in patients ≤18 years of age than in those aged >18 years (55.56% vs. 9.17%, χ² = 0.55, p < 0.027). Patients with allergic rhinitis and asthma had an increased positive rate for Betula pollen allergen (20.00% vs. 37.93 χ² = 7.87, p = 0.005) and Platanus pollen allergen (27.27% vs. 51.72%, χ² = 11.05, p = 0.0008) than those with allergic rhinitis alone, although the allergen positivity rate did not significantly differ between sexes. In addition, the positivity of sIgE of allergen components did not reveal a correlation with clinical symptoms and anti-CCD IgE positivity was 1.19% (1/84) among all patients.ConclusionThe study found the distribution characteristics of common pollen allergens in Beijing among patients of different ages and genders and with different allergic diseases, as well as the relationship between pollen allergen components and symptoms. The positivity rate of CCD for respiratory allergic diseases in Beijing was not high as well.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1454292</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1454292</link>
        <title><![CDATA[The Acari Hypothesis, V: deciphering allergenicity]]></title>
        <pubdate>2024-11-01T00:00:00Z</pubdate>
        <category>Hypothesis and Theory</category>
        <author>Andrew C. Retzinger</author><author>Gregory S. Retzinger</author>
        <description><![CDATA[The Acari Hypothesis posits that acarians, i.e., mites and ticks, are operative agents of allergy. It derived from observations that allergens are molecular elements of acarians or acarian foodstuffs. A corollary of The Hypothesis provides how acarian dietary elements are selected as allergens; namely, a pattern recognition receptor native to the acarian digestive tract complexes with dietary molecules problematic to the acarian. By virtue of its interspecies operability, the receptor then enables not only removal of the dietary elements by the acarian immune system, but also—should such a complex be inoculated into a human—production of an element-specific IgE. Because pattern recognition receptors bind to molecules problematic to the organism from which the receptors originate, it follows that molecules targeted by adaptive IgE, i.e., allergens, must be problematic to acarians. This claim is supported by evidence that host organisms, when infested by acarians, upregulate representative members of allergenic molecular families. Appreciation of the relationship between allergens and acarians provides insight well beyond allergy, shedding light also on the anti-acarian defenses of many living things, especially humans.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1483398</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1483398</link>
        <title><![CDATA[Editorial: In vitro diagnosis of allergic and mast cell-mediated disorders]]></title>
        <pubdate>2024-10-25T00:00:00Z</pubdate>
        <category>Editorial</category>
        <author>Joana Vitte</author><author>Alexandra F. Santos</author>
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1481011</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1481011</link>
        <title><![CDATA[Allergenic protein-induced type I hypersensitivity models: a review]]></title>
        <pubdate>2024-10-17T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Yanhua Feng</author><author>Liangyu Xu</author><author>Jinming Zhang</author><author>Jinlian Bin</author><author>Xialing Pang</author><author>Sheng He</author><author>Lei Fang</author>
        <description><![CDATA[ContextType I hypersensitivity affects approximately one-third of the global population. As the pathophysiology underlying the development of type I hypersensitivity (asthma, food allergy, and anaphylactic shock, etc.) is complex and heterogeneous, animal model studies continue to be the key to identifying novel molecular pathways and providing therapeutic strategies.ObjectiveSelection of the animal model should be done with careful consideration of the protocol variables, animal species, and strains to accurately reflect the clinical symptoms typical of humans.MethodsThe following databases were searched: PubMed and Web of Science.Results and conclusionForeign allergens include allergenic proteins and chemical haptens. This review summarizes the various methods used for designing animal models of common allergenic protein-induced type I hypersensitivity, namely, passive anaphylaxis model, active systemic anaphylaxis/anaphylaxis shock model, food allergy model, asthma model, and IgE-mediated cell models. Additionally, we summarize shrimp tropomyosin-induced type I hypersensitivity models from our previous studies and discuss their advantages and limitations compared with that of ovalbumin-induced models.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1466954</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1466954</link>
        <title><![CDATA[Editorial: Allergen source-specific mucosal barrier disruptors]]></title>
        <pubdate>2024-08-12T00:00:00Z</pubdate>
        <category>Editorial</category>
        <author>Rajna Minić</author><author>Lidija Burazer</author><author>Andrijana Nešić</author><author>Sabine Flicker</author>
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1469718</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1469718</link>
        <title><![CDATA[Editorial: The regulation of allergic responses by proteolysis: from protease allergens to host proteases modulation]]></title>
        <pubdate>2024-08-12T00:00:00Z</pubdate>
        <category>Editorial</category>
        <author>Wai Tuck Soh</author><author>Alain Jacquet</author>
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1440360</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1440360</link>
        <title><![CDATA[To stay or not to stay intact as an allergen: the endolysosomal degradation assay used as tool to analyze protein immunogenicity and T cell epitopes]]></title>
        <pubdate>2024-07-12T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Elif Öztemiz Topcu</author><author>Gabriele Gadermaier</author>
        <description><![CDATA[Antigen uptake and processing of exogenous proteins is critical for adaptive immunity, particularly for T helper cell activation. Proteins undergo distinct proteolytic processing in endolysosomal compartments of antigen-presenting cells. The resulting peptides are presented on MHC class II molecules and specifically recognized by T cells. The in vitro endolysosomal degradation assay mimics antigen processing by incubating a protein of interest with a protease cocktail derived from the endolysosomal compartments of antigen presenting cells. The kinetics of protein degradation is monitored by gel electrophoresis and allows calculation of a protein's half-life and thus endolysosomal stability. Processed peptides are analyzed by mass spectrometry and abundant peptide clusters are shown to harbor T cell epitopes. The endolysosomal degradation assay has been widely used to study allergens, which are IgE-binding proteins involved in type I hypersensitivity. In this review article, we provide the first comprehensive overview of the endolysosomal degradation of 29 isoallergens and variants originating from the PR-10, Ole e 1-like, pectate lyase, defensin polyproline-linked, non-specific lipid transfer, mite group 1, 2, and 5, and tropomyosin protein families. The assay method is described in detail and suggestions for improved standardization and reproducibility are provided. The current hypothesis implies that proteins with high endolysosomal stability can induce an efficient immune response, whereas highly unstable proteins are degraded early during antigen processing and therefore not efficient for MHC II peptide presentation. To validate this concept, systematic analyses of high and low allergenic representatives of protein families should be investigated. In addition to purified molecules, allergen extracts should be degraded to analyze potential matrix effects and gastrointestinal proteolysis of food allergens. In conclusion, individual protein susceptibility and peptides obtained from the endolysosomal degradation assay are powerful tools for understanding protein immunogenicity and T cell reactivity. Systematic studies and linkage with in vivo sensitization data will allow the establishment of (machine-learning) tools to aid prediction of immunogenicity and allergenicity. The orthogonal method could in the future be used for risk assessment of novel foods and in the generation of protein-based immunotherapeutics.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2024.1426816</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2024.1426816</link>
        <title><![CDATA[Spatiotemporal proteolytic susceptibility of allergens: positive or negative effects on the allergic sensitization?]]></title>
        <pubdate>2024-07-09T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Alain Jacquet</author><author>Wai Tuck Soh</author>
        <description><![CDATA[From their expression in their respective allergenic source to their processing by antigen presenting cells, allergens continuously encounter proteases. The ability of allergens to resist to proteolysis by digestive enzymes or host-cell/microbial proteases is considered as an important property that influences their allergenic potential. However, the relationship between proteolytic stability and allergenicity is much more complex and depends on various factors, such as the protein structure dynamics, the exposure level, the route of sensitization, and their respective protease susceptibility. In this review, we summarize and discuss the current knowledge on several aspects of allergen proteolytic stability in different environments including the allergenic sources, routes of sensitization (skin, respiratory tract, gastrointestinal tract) and endolysosomal compartment of antigen-presenting cells. Proteolytic stability alone cannot represent a definitive criterion to allergenicity. The proteolytic susceptibility of allergens in processed extracts can affect allergy diagnosis and immunotherapy. Furthermore, the fine tuning of allergen stability during antigen processing can be exploited for the development of novel immunotherapeutic strategies.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1322117</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1322117</link>
        <title><![CDATA[Case Report: A family history of peanut allergy and hereditary alpha-tryptasemia]]></title>
        <pubdate>2024-01-23T00:00:00Z</pubdate>
        <category>Case Report</category>
        <author>Yannick Chantran</author><author>Hélène Renaudin</author><author>Michel Arock</author><author>Tamazoust Guiddir</author><author>Ariane Nemni</author>
        <description><![CDATA[ContextHereditary alpha-tryptasemia (HαT) is associated with elevated basal serum tryptase (bST) and is associated with a higher risk of severe anaphylactic reactions in patients with clonal mast cell disorders or IgE-mediated Hymenoptera venom-induced anaphylaxis. The consequence of this genetic trait remains to be determined in other allergic diseases and food allergy in particular.ObjectivesHere, we describe three cases of peanut allergy among siblings from a single family of four: two of them were associated with HαT, and the third one was associated with the tryptase wild-type genotype.MethodsTPSAB1/TPSB2 genotypes were determined by digital PCR. After the case description, we provided a review of the literature regarding bST levels and tryptase genotypes in anaphylaxis, with a particular focus on food allergy.ResultsCompared to the sibling with the conventional tryptase genotype, the two siblings with HαT presented a lower peanut threshold at the initial oral food challenge, higher peanut skin prick test reactivity, higher levels of specific IgE to peanut, Ara h 2, and Ara h 6, and a lower IgG4/IgE ratio after 10 years of oral immunotherapy.ConclusionThe tryptase genotype and HαT status might modify the clinical presentation and biological features of food allergy.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1339678</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1339678</link>
        <title><![CDATA[Editorial: Allergic sensitization in infants]]></title>
        <pubdate>2023-12-04T00:00:00Z</pubdate>
        <category>Editorial</category>
        <author>Kirsi M. Järvinen</author><author>Nitya Jain</author><author>Daniel Munblit</author><author>R. J. Joost van Neerven</author>
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1270326</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1270326</link>
        <title><![CDATA[Unique allergen-specific human IgE monoclonal antibodies derived from patients with allergic disease]]></title>
        <pubdate>2023-10-12T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Bryan R. E. Smith</author><author>Kristina Reid Black</author><author>Max Bermingham</author><author>Sayeh Agah</author><author>Jill Glesner</author><author>Serge A. Versteeg</author><author>Ronald van Ree</author><author>Glorismer Pena-Amelunxen</author><author>Lorenz Aglas</author><author>Scott A. Smith</author><author>Anna Pomés</author><author>Martin D. Chapman</author>
        <description><![CDATA[IntroductionAllergic reactions are mediated by human IgE antibodies that bind to and cross-link allergen molecules. The sites on allergens that are recognized by IgE antibodies have been difficult to investigate because of the paucity of IgE antibodies in a human serum. Here, we report the production of unique human IgE monoclonal antibodies to major inhaled allergens and food allergens that can be produced at scale in perpetuity.Materials and methodsThe IgE antibodies were derived from peripheral blood mononuclear cells of symptomatic allergic patients, mostly children aged 3–18 years, using hybridoma fusion technology. Total IgE and allergen-specific IgE was measured by ImmunoCAP. Their specificity was confirmed through ELISA and immunoblotting. Allergenic potency measurements were determined by ImmunoCAP inhibition. Biological activity was determined in vitro by comparing β-hexosaminidase release from a humanized rat basophilic cell line.ResultsHuman IgE monoclonal antibodies (n = 33) were derived from 17 allergic patients with symptoms of allergic rhinitis, asthma, atopic dermatitis, food allergy, eosinophilic esophagitis, or red meat allergy. The antibodies were specific for five inhaled allergens, nine food allergens, and alpha-gal and had high levels of IgE (53,450–1,702,500 kU/L) with ratios of specific IgE to total IgE ranging from <0.01 to 1.39. Sigmoidal allergen binding curves were obtained through ELISA, with low limits of detection (<1 kU/L). Allergen specificity was confirmed through immunoblotting. Pairs of IgE monoclonal antibodies to Ara h 6 were identified that cross-linked after allergen stimulation and induced release of significant levels of β-hexosaminidase (35%–80%) from a humanized rat basophilic cell line.ConclusionsHuman IgE monoclonal antibodies are unique antibody molecules with potential applications in allergy diagnosis, allergen standardization, and identification of allergenic epitopes for the development of allergy therapeutics. The IgE antibody probes will enable the unequivocal localization and validation of allergenic epitopes.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1265049</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1265049</link>
        <title><![CDATA[Sensing of protease activity as a triggering mechanism of Th2 cell immunity and allergic disease]]></title>
        <pubdate>2023-09-21T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Audrey Meloun</author><author>Beatriz León</author>
        <description><![CDATA[CD4 T-helper cell type 2 (Th2) cells mediate host defense against extracellular parasites, like helminths. However, Th2 cells also play a pivotal role in the onset and progression of allergic inflammatory diseases such as atopic dermatitis, allergic rhinitis, asthma, and food allergy. This happens when allergens, which are otherwise harmless foreign proteins, are mistakenly identified as “pathogenic.” Consequently, the encounter with these allergens triggers the activation of specific Th2 cell responses, leading to the development of allergic reactions. Understanding the molecular basis of allergen sensing is vital for comprehending how Th2 cell responses are erroneously initiated in individuals with allergies. The presence of protease activity in allergens, such as house dust mites (HDM), pollen, fungi, or cockroaches, has been found to play a significant role in triggering robust Th2 cell responses. In this review, we aim to examine the significance of protease activity sensing in foreign proteins for the initiation of Th2 cell responses, highlighting how evolving a host protease sensor may contribute to detect invading helminth parasites, but conversely can also trigger unwanted reactions to protease allergens. In this context, we will explore the recognition receptors activated by proteolytic enzymes present in major allergens and their contribution to Th2-mediated allergic responses. Furthermore, we will discuss the coordinated efforts of sensory neurons and epithelial cells in detecting protease allergens, the subsequent activation of intermediary cells, including mast cells and type 2 innate lymphoid cells (ILC2s), and the ultimate integration of all signals by conventional dendritic cells (cDCs), leading to the induction of Th2 cell responses. On the other hand, the review highlights the role of monocytes in the context of protease allergen exposure and their interaction with cDCs to mitigate undesirable Th2 cell reactions. This review aims to provide insights into the innate functions and cell communications triggered by protease allergens, which can contribute to the initiation of detrimental Th2 cell responses, but also promote mechanisms to effectively suppress their development.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1239924</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1239924</link>
        <title><![CDATA[Allergy patient-specific IgE antibody shows significantly stability during 3 months of storage at multiple temperatures from −80 to 25°C]]></title>
        <pubdate>2023-09-07T00:00:00Z</pubdate>
        <category>Brief Research Report</category>
        <author>Zhifeng Huang</author><author>Huiqing Zhu</author><author>Lexin Xiao</author><author>Tingting Liu</author><author>Hui Gan</author><author>Runpei Lin</author><author>Wenting Luo</author><author>Baoqing Sun</author>
        <description><![CDATA[The detection of allergen-specific IgE antibodies is an important biomarker for the diagnosis and treatment monitoring of allergic diseases. And the pre-analytical phase is an important part of the overall quality of the laboratory. In this study, 44 patients with allergic diseases (including 23 patients with allergic rhinitis, 12 patients with allergic rhinitis and asthma, and 9 patients with allergic dermatitis) were included in the outpatient center of the Department of Allergy, the First Affiliated Hospital of Guangzhou Medical University. We mixed the serums of the above 44 patients (approximately 0.8 ml of serum volume per patient) into a large volume of serum pool (about 35 ml in total) and divided into 26 parts. And 26 serum samples were stored at 4 different temperatures for 90 days to observe the stability of sIgE antibodies to 16 allergens in serum. The results show that serum sIgE antibody titers in patients with allergic diseases show significant stability during 90 days of storage, even at room temperature. Good stability even after up to 10 freeze-thaw cycles under low temperature storage conditions.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1260902</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1260902</link>
        <title><![CDATA[Molecular allergology and its application in prevention, diagnosis and therapy]]></title>
        <pubdate>2023-08-07T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Aleksandra Podzhilkova</author><author>Christoph Nagl</author><author>Karin Hoffmann-Sommergruber</author>
        <description><![CDATA[Allergic diseases represent a relevant global health problem, affecting adults and children and posing a significant burden for health care systems. In addition, the disease is still under-recognized and harmonized diagnostic tools and management plans for patients are still lacking. In this review the most important aspects of the diagnosis of allergic diseases are summarized and the contribution of Molecular allergology to this area is highlighted.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/falgy.2023.1173540</guid>
        <link>https://www.frontiersin.org/articles/10.3389/falgy.2023.1173540</link>
        <title><![CDATA[Early inhalant allergen sensitization at component level: an analysis in atopic Dutch children]]></title>
        <pubdate>2023-06-27T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Lonneke J. Landzaat</author><author>Joyce A. M. Emons</author><author>Laura J. H. Sonneveld</author><author>Marco W. J. Schreurs</author><author>Nicolette J. T. Arends</author>
        <description><![CDATA[BackgroundAllergic rhinitis is a common respiratory disease in children and sensitization to inhalant allergens plays a significant role in its development. However, limited knowledge exists regarding sensitization profiles of inhalant allergen components in atopic children, particularly in the very young individuals. Understanding these profiles could provide insights into the early development of allergic rhinitis. The objective of this cross-sectional retrospective study was to evaluate the IgE-sensitization profiles to multiple inhalant allergen components and their clinical relevance in Dutch atopic children, with specific focus on children under the age of 4 years.MethodsA total of 243 atopic children were included in the study and sensitization profiles were analyzed using multiplex microarray analysis (ISAC). Clinical information was obtained from records of a pediatric allergy outpatient clinic between 2011 and 2020. Specific IgE responses to inhalation allergen components from five allergen sources (grass pollen, tree pollen, house dust mite, cat and dog), were examined. The study encompassed children of different age groups and compared those with and without symptoms.ResultsThe results demonstrated that sensitization to inhalant allergen components was present in 92% of the cohort. Sensitization was already evident at a young age (87%), including infancy, with a rapid increase in prevalence after 1 year of age. House dust mite emerged as the most predominant sensitizing allergen in early childhood, followed by tree pollen in later years. Sensitization patterns were similar between symptomatic and asymptomatic children, although symptomatic children exhibited higher frequencies and values. The sensitization profiles in very young children were comparable to those of children across all age groups.ConclusionThese findings highlight the presence of sensitization to inhalant allergen components and the early onset of allergic rhinitis before the age of 4, including infancy, in Dutch atopic children. Notable allergen molecules in Dutch atopic children under the age of 4 years include Bet v 1, Fel d 1, Der f 1, Der p 1, Der p 10 and Phl p 4, with house dust mite sensitization being the most common among Dutch infants. Moreover, the prevalence of sensitization to inhalant allergens in this Dutch cohort surpassed that of general European populations, emphasizing the importance of early assessment and management of allergic rhinitis in young atopic children.]]></description>
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