Immunoinformatics Construction of B Cell Epitope-Based Hypoallergenic Der f 34 Vaccine for Immunotherapy of House Dust Mite Allergy

Yu, Pengfei; Zhu, Ying; Tan, Lingxiao; Xu, Zhi‐Qiang; Chen, Lu; Guan, Xiaowei

doi:10.1007/s10989-021-10337-2

Cited by 3 publications

(3 citation statements)

References 36 publications

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“…A similar alternative to abolishing IgE binding and retaining anaphylactogenic potency was proposed by Tscheppe et al (2020). Yu et al (2022) recently converted the major house dust mite allergen Der f 34 into a B cell epitope-based hypoallergenic vaccine based on immunoinformatics and peptide-carrier fusion approaches. Three different fragments of major allergen Der f 34 that contained candidate B cell epitope and without T cell epitopes were linked at the N terminal and C terminal of the PreS carrier, and the interaction with immune receptors (toll-like receptor-3) by ligand-receptor docking were evaluated.…”

Section: Discussionmentioning

confidence: 97%

Production of a Ric c3 hypo-allergen with no IgE binding or anaphylactogenic activity

Bartholazzi,

Lodi,

Mello

et al. 2023

Braz. J. Biol.

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Several studies have been carried out to expand the use of Ricinus communis L. castor bean (Ricinus communis L castor bean.). This oilseed finds appropriate conditions for its development in Brazil, with more than 700 applications. The main allergens of this plant are Ric c1 and Ric c3, that cross-react with various aeroallergens and food allergens such as peanuts, soybeans, corn, and wheat. This study aimed to determine the effect of mutations in Ric c3 amino acid residues known to affect IgE binding and allergy challenges. Based on the Ric c3 structure, B-cell epitopes, and amino acid involved in IgE binding, we produce recombinant mutant protein, mrRic c3, secreted from E. coli. Strategic glutamic acid residues in IgE-biding regions were changed by Leucine. The allergenicity of mrRic c3 was evaluated by determination of IgE, IgG1, and total IgG in immunized Balb/c mice and by degranulation assays of mast cells isolated from Wistar rats. The mrRic c3 presented a percentage of mast cell degranulation close to that seen in the negative control, and the immunization of mice with mrRic c3 presented lower levels of IgE and IgG1 than the group treated with the protein without mutations. The mutant mrRic c3 had an altered structure and reduced ability to stimulate pro-inflammatory responses and bind IgE but retained its ability to induce blocking antibodies. Thus, producing a hypoallergenic mutant allergen (mrRic c3) may be essential in developing new AIT strategies.

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Section: Discussionmentioning

confidence: 97%

Production of a Ric c3 hypo-allergen with no IgE binding or anaphylactogenic activity

Bartholazzi,

Lodi,

Mello

et al. 2023

Braz. J. Biol.

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“…Identity of protein sequences along with structural epitopes play an important role in predicting crossreactivity (Yu, 2022). For protein sequence identity, it has been observed that there is at least 70% sequence identity between two cross-reacting allergens (RC, 2000).…”

Section: Discussionmentioning

confidence: 99%

Identification and Annotation of Peptide Allergens in Prunus dulcis

Singh

Upadhyay²

2022

Int J Pept Res Ther

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Approximately, 10% of the world population is facing the challenge of food allergy in direct or indirect way. In this study, a genome-wide identi cation and annotation of the novel putative allergen from Almond is performed. Initially, the whole proteome of Almond (31,000 proteins) was scanned by Allergenonline, a publically available database of already reported allergens from different sources. The detailed analysis suggests that there are 430 putative allergens which reduced to 45 on motif-based screening using AllFam database. These predicted allergens are annotated for their function by using PFAM, GO databases and orthology analysis. To validate our prediction, we have used structural insights of allergen and antibody interactions for one of the predicted putative allergen protein, homologous to Pru ar 3.0101allergen from Apricot. The structure of putative allergen was modeled and molecular docking studies were performed against the antibody. The best docked conformation was subjected to molecular simulation studies to con rm the stable binding of these two molecules. This detailed analysis suggests that the identi ed allergen will show cross reactivity similar to Pru ar 3.0101 allergen from Apricot. This is one of the rst report of identifying and annotating the homologous of Pru ar 3.0101 allergen in Almond.

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“…Previous studies have highlighted the significance of groups 1, 2, and 23 in HDM as the most crucial allergens ( 20 ). Most hypoallergenic vaccine studies focused on the major allergens and individualized therapy for mite allergy ( 21 ). Der f 36 is a newly identified HDM allergen in recent years.…”

Section: Introductionmentioning

confidence: 99%

Construction by artificial intelligence and immunovalidation of hypoallergenic mite allergen Der f 36 vaccine

Qin,

Tang,

Wang

et al. 2024

Front. Immunol.

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BackgroundThe house dust mite (HDM) is widely recognized as the most prevalent allergen in allergic diseases. Allergen-specific immunotherapy (AIT) has been successfully implemented in clinical treatment for HDM. Hypoallergenic B-cell epitope-based vaccine designed by artificial intelligence (AI) represents a significant progression of recombinant hypoallergenic allergen derivatives.MethodThe three-dimensional protein structure of Der f 36 was constructed using Alphafold2. AI-based tools were employed to predict B-cell epitopes, which were subsequently verified through IgE-reaction testing. Hypoallergenic Der f 36 was then synthesized, expressed, and purified. The reduced allergenicity was assessed by enzyme-linked immunosorbent assay (ELISA), immunoblotting, and basophil activation test. T-cell response to hypoallergenic Der f 36 and Der f 36 was evaluated based on cytokine expression in the peripheral blood mononuclear cells (PBMCs) of patients. The immunogenicity was evaluated and compared through rabbit immunization with hypoallergenic Der f 36 and Der f 36, respectively. The inhibitory effect of the blocking IgG antibody on the specific IgE-binding activity and basophil activation of Der f 36 allergen was also examined.ResultsThe final selected non-allergic B-cell epitopes were 25–48, 57–67, 107–112, 142–151, and 176–184. Hypoallergenic Der f 36 showed significant reduction in IgE-binding activity. The competitive inhibition of IgE-binding to Der f 36 was investigated using the hypoallergenic Der f 36, and only 20% inhibition could be achieved, which is greatly reduced when compared with inhibition by Der f 36 (98%). The hypoallergenic Der f 36 exhibited a low basophil-stimulating ratio similar to that of the negative control, and it could induce an increasing level of IFN‐γ but not Th2 cytokines IL-5 and IL-13 in PBMCs. The vaccine-specific rabbit blocking IgG antibodies could inhibit the patients’ IgE binding and basophil stimulation activity of Derf 36.ConclusionThis study represents the first application of an AI strategy to facilitate the development of a B-cell epitope-based hypoallergenic Der f 36 vaccine, which may become a promising immunotherapy for HDM-allergic patients due to its reduced allergenicity and its high immunogenicity in inducing blocking of IgG.

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Immunoinformatics Construction of B Cell Epitope-Based Hypoallergenic Der f 34 Vaccine for Immunotherapy of House Dust Mite Allergy

Cited by 3 publications

References 36 publications

Production of a Ric c3 hypo-allergen with no IgE binding or anaphylactogenic activity

Production of a Ric c3 hypo-allergen with no IgE binding or anaphylactogenic activity

Identification and Annotation of Peptide Allergens in Prunus dulcis

Construction by artificial intelligence and immunovalidation of hypoallergenic mite allergen Der f 36 vaccine

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