ArticleJournal of clinical immunology2009
Engineered Alt a 13 fragment of Alternaria alternata abrogated IgE binding without affecting T-cell stimulation.
Article in Journal of clinical immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Changes in the Sensitization Pattern toJournal of fungi (Basel, Switzerland) · 2021Article
- Preclinical safety and immunological efficacy of Alternaria alternata polymerized extracts.Immunity, inflammation and disease · 2018Article
- Mold allergens in respiratory allergy: from structure to therapy.Allergy, asthma & immunology research · 2015Review
- Alternaria alternata and its allergens: a comprehensive review.Clinical reviews in allergy & immunology · 2014Review
- Characterization of recombinant per a 10 from Periplaneta americana.Clinical and vaccine immunology : CVI · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
rationaleEpitopes were delineated for allergenic proteins, but studies are required to identify residues mediating IgE binding. In the present study, the in silico approach was used to identify IgE-binding residues of Alt a 13(1-50) fragment and confirmed by experimental approach. METHOD AND
resultsIgE-binding epitopes of Alt a 13 mapped computationally were cloned, expressed, purified, and characterized using various immunochemical and biophysical methods. Among four fragments of Alt a 13, Alt a 13(1-50) demonstrated maximum IgE binding with two immunodominant regions and was mutated at these regions. The mutation in first region, Alt a 13(1-50)-K4A_S6F, did not show any change in immunological and biophysical properties of protein. However, mutations in the second region, Alt a 13(1-50)-T21F_N27I, caused reduced IgE binding, histamine release, and low IL-4 release on stimulation of Alternaria alternata positive patients peripheral blood mononuclear cells in vitro.
conclusionThis suggests that residues T21 and N27 are important for the secondary structure. In conclusion, Alt a 13(1-50)-T21F_N27I with reduced Th 2 response and intact T-cell proliferation capacity has potential for clinical use.
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