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Deciphering Allergies—Structural and Immunological Characterization of Allergenic Proteins and Immunomodulatory Agents

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Immunology".

Deadline for manuscript submissions: 30 September 2024 | Viewed by 2844

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Special Issue Editors

Dr. Marija Gavrović-Jankulović

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Guest Editor

Department of Biochemistry, Faculty of Chemistry, University of Belgrade, Belgrade, Serbia
Interests: molecular allergology; immunology

Dr. Danijela Apostolović

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Guest Editor

Immunology and Allergy Division, Department of Medicine Solna, Karolinska Insititutet, Stockholm, Sweden
Interests: molecular allergology; immunology

Special Issue Information

Dear Colleagues,

Allergies are one of today's most common immune disorders; this is mostly because of an exaggerated immunoglobulin E-mediated immune response to harmless environmental allergens. The main translational goal to study allergies is to understand immune mechanisms, improve diagnosis, find a better and reliable immunotherapy, and manage the disease. Other factors, such as exposomes (parasites, ticks, drugs, heavy metals, plastic, and other contaminants) represent novel elements that act as important immunomodulatory agents in the allergic diseases and should be further investigated.

Therefore, the basis to achieve these goals are in the structural and immunological characterization of allergenic proteins; the interplay between allergens and innate and adaptive immunity; the development of novel therapeutic approaches; and the investigation of exposomes as immunomodulatory agents.

Potential topics include but are not limited to:

Allergens: new and old epitopes enrolled in IgE binding and allergenicity;
In silico discovery of allergens and prediction of allergenicity and allergic cross-reactivity;
Allergenicity prediction of novel foods;
Modulation of immune response by designed allergenic proteins;
Allergen structure interplay with the innate immunity;
Parasites and vectors as allergen transmitters;
Effects of environmental pollutants on allergenicity;
Effects of micro- and nano-plastics on protein allergenicity.

Dr. Marija Gavrović-Jankulović
Dr. Danijela Apostolović
Guest Editors

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Keywords

allergen
allergenicity
IgE
innate immunity
exposome
cross-reactivity
B cell epitopes
T cell epitopes
in silico prediction

Published Papers (4 papers)

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Research

18 pages, 2361 KiB

Open AccessArticle

Non-Specific Lipid Transfer Protein Amb a 6 Is a Source-Specific Important Allergenic Molecule in Ragweed Pollen

by Manuela Grijincu, Gabriela Tănasie, Lauriana-Eunice Zbîrcea, Maria-Roxana Buzan, Tudor-Paul Tamaș, Monica-Daniela Cotarcă, Ioan Huțu, Elijahu Babaev, Frank Stolz, Yulia Dorofeeva, Rudolf Valenta, Virgil Păunescu, Carmen Panaitescu and Kuan-Wei Chen

Int. J. Mol. Sci. 2024, 25(12), 6513; https://doi.org/10.3390/ijms25126513 - 13 Jun 2024

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Abstract

Pollen from common ragweed is an important allergen source worldwide and especially in western and southern Romania. More than 100 million patients suffer from symptoms of respiratory allergy (e.g., rhinitis, asthma) to ragweed pollen. Among the eleven characterized allergens, Amb a 6 is a non-specific lipid transfer protein (nsLTP). nsLTPs are structurally stable proteins in pollen and food from different unrelated plants capable of inducing severe reactions. The goal of this study was to produce Amb a 6 as a recombinant and structurally folded protein (rAmb a 6) and to characterize its physicochemical and immunological features. rAmb a 6 was expressed in Spodoptera frugiperda Sf9 cells as a secreted protein and characterized by mass spectrometry and circular dichroism (CD) spectroscopy regarding molecular mass and fold, respectively. The IgE-binding frequency towards the purified protein was evaluated using sera from 150 clinically well-characterized ragweed-allergic patients. The allergenic activities of rAmb a 6 and the nsLTP from the weed Parietaria judaica (Par j 2) were evaluated in basophil activation assays. rAmb a 6-specific IgE reactivity was associated with clinical features. Pure rAmb a 6 was obtained by insect cell expression. Its deduced molecular weight corresponded to that determined by mass spectrometry (i.e., 10,963 Da). rAmb a 6 formed oligomers as determined by SDS-PAGE under non-reducing conditions. According to multiple sequence comparisons, Amb a 6 was a distinct nsLTP with less than 40% sequence identity to currently known plant nsLTP allergens, except for nsLTP from Helianthus (i.e., 52%). rAmb a 6 is an important ragweed allergen recognized by 30% of ragweed pollen allergic patients. For certain patients, rAmb a 6-specific IgE levels were higher than those specific for the major ragweed allergen Amb a 1 and analysis also showed a higher allergenic activity in the basophil activation test. rAmb a 6-positive patients suffered mainly from respiratory symptoms. The assumption that Amb a 6 is a source-specific ragweed allergen is supported by the finding that none of the patients showing rAmb a 6-induced basophil activation reacted with Par j 2 and only one rAmb a 6-sensitized patient had a history of plant food allergy. Immunization of rabbits with rAmb a 6 induced IgG antibodies which strongly inhibited IgE binding to rAmb a 6. Our results demonstrate that Amb a 6 is an important source-specific ragweed pollen allergen that should be considered for diagnosis and allergen-specific immunotherapy of ragweed pollen allergy. Full article

(This article belongs to the Special Issue Deciphering Allergies—Structural and Immunological Characterization of Allergenic Proteins and Immunomodulatory Agents)

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16 pages, 4198 KiB

Open AccessArticle

Utilizing the Banana S-Adenosyl-L-Homocysteine Hydrolase Allergen to Identify Cross-Reactive IgE in Ryegrass-, Latex-, and Kiwifruit-Allergic Individuals

by Tatjana Đurašinović, Zorana Lopandić, Isidora Protić-Rosić, Tina Ravnsborg, Gordan Blagojević, Lidija Burazer, Ole N. Jensen and Marija Gavrović-Jankulović

Int. J. Mol. Sci. 2024, 25(11), 5800; https://doi.org/10.3390/ijms25115800 - 26 May 2024

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Abstract

Food allergies mediated by specific IgE (sIgE) have a significant socioeconomic impact on society. Evaluating the IgE cross-reactivity between allergens from different allergen sources can enable the better management of these potentially life-threatening adverse reactions to food proteins and enhance food safety. A novel banana fruit allergen, S-adenosyl-L-homocysteine hydrolase (SAHH), has been recently identified and its recombinant homolog was heterologously overproduced in E. coli. In this study, we performed a search in the NCBI (National Center for Biotechnology Information) for SAHH homologs in ryegrass, latex, and kiwifruit, all of which are commonly associated with pollen-latex-fruit syndrome. In addition, Western immunoblot analysis was utilized to identify the cross-reactive IgE to banana SAHH in the sera of patients with a latex allergy, kiwifruit allergy, and ryegrass allergy. ClustalOmega analysis showed more than 92% amino acid sequence identity among the banana SAHH homologs in ryegrass, latex, and kiwifruit. In addition to five B-cell epitopes, in silico analysis predicted eleven T-cell epitopes in banana SAHH, seventeen in kiwifruit SAHH, twelve in ryegrass SAHH, and eight in latex SAHH, which were related to the seven-allele HLA reference set (HLA-DRB1*03:01, HLA-DRB1*07:01, HLA-DRB1*15:01, HLA-DRB3*01:01, HLA-DRB3*02:02, HLA-DRB4*01:01, HLA-DRB5*01:01). Four T-cell epitopes were identical in banana and kiwifruit SAHH (positions 328, 278, 142, 341), as well as banana and ryegrass SAHH (positions 278, 142, 96, and 341). All four SAHHs shared two T-cell epitopes (positions 278 and 341). In line with the high amino acid sequence identity and B-cell epitope homology among the analyzed proteins, the cross-reactive IgE to banana SAHH was detected in three of three latex-allergic patients, five of six ryegrass-allergic patients, and two of three kiwifruit-allergic patients. Although banana SAHH has only been studied in a small group of allergic individuals, it is a novel cross-reactive food allergen that should be considered when testing for pollen-latex-fruit syndrome. Full article

(This article belongs to the Special Issue Deciphering Allergies—Structural and Immunological Characterization of Allergenic Proteins and Immunomodulatory Agents)

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16 pages, 2244 KiB

Open AccessArticle

Insect Cell-Expressed Major Ragweed Allergen Amb a 1.01 Exhibits Similar Allergenic Properties to Its Natural Counterpart from Common Ragweed Pollen

by Maria-Roxana Buzan, Manuela Grijincu, Lauriana-Eunice Zbîrcea, Laura Haidar, Tudor-Paul Tamaș, Monica-Daniela Cotarcă, Gabriela Tănasie, Milena Weber, Elijahu Babaev, Frank Stolz, Rudolf Valenta, Virgil Păunescu, Carmen Panaitescu and Kuan-Wei Chen

Int. J. Mol. Sci. 2024, 25(10), 5175; https://doi.org/10.3390/ijms25105175 - 9 May 2024

Viewed by 553

Abstract

Common ragweed pollen allergy has become a health burden worldwide. One of the major allergens in ragweed allergy is Amb a 1, which is responsible for over 90% of the IgE response in ragweed-allergic patients. The major allergen isoform Amb a 1.01 is the most allergenic isoform in ragweed pollen. So far, no recombinant Amb a 1.01 with similar allergenic properties to its natural counterpart (nAmb a 1.01) has been produced. Hence, this study aimed to produce a recombinant Amb a 1.01 with similar properties to the natural isoform for improved ragweed allergy management. Amb a 1.01 was expressed in insect cells using a codon-optimized DNA construct with a removable N-terminal His-Tag (rAmb a 1.01). The recombinant protein was purified by affinity chromatography and physicochemically characterized. The rAmb a 1.01 was compared to nAmb a 1.01 in terms of the IgE binding (enzyme-linked immunosorbent assay (ELISA), immunoblot) and allergenic activity (mediator release assay) in well-characterized ragweed-allergic patients. The rAmb a 1.01 exhibited similar IgE reactivity to nAmb a 1.01 in different IgE-binding assays (i.e., IgE immunoblot, ELISA, quantitative ImmunoCAP inhibition measurements). Furthermore, the rAmb a 1.01 showed comparable dose-dependent allergenic activity to nAmb a 1.01 regarding basophil activation. Overall, the results showed the successful expression of an rAmb a 1.01 with comparable characteristics to the corresponding natural isoform. Our findings provide the basis for an improvement in ragweed allergy research, diagnosis, and immunotherapy. Full article

(This article belongs to the Special Issue Deciphering Allergies—Structural and Immunological Characterization of Allergenic Proteins and Immunomodulatory Agents)

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14 pages, 1492 KiB

Open AccessArticle

Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR

by Mirjana Radomirović, Nikola Gligorijević, Dragana Stanić-Vučinić, Andreja Rajković and Tanja Ćirković Veličković

Int. J. Mol. Sci. 2023, 24(20), 15410; https://doi.org/10.3390/ijms242015410 - 21 Oct 2023

Viewed by 1068

Abstract

Tropomyosin is the major and predominant allergen among shellfish. This study developed an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods. The method couples sandwich ELISA with the real-time PCR (rtPCR) amplification of marker DNAs. Monoclonal anti-TPM antibody was the capture antibody, polyclonal rabbit anti-shrimp tropomyosin antibody was the detection antibody, while natural shrimp tropomyosin served as the standard. A double-stranded amino-DNA was covalently conjugated to a secondary anti-rabbit antibody and subsequently amplified and quantified via rtPCR. The quantification sensitivity of immuno-PCR was 20-fold higher than analogous ELISA, with LOQ 19.8 pg/mL. The developed immuno-PCR method is highly specific for the detection of crustacean tropomyosin and is highly precise in a broad concentration range. Tropomyosin recovery in the spiked vegetable soup was 87.7–115.6%. Crustacean tropomyosin was also quantified in commercial food products. The reported immuno-PCR assay is the most sensitive method for the quantification of crustacean tropomyosin and is the first immuno-PCR-based assay for the quantification of food allergen and food protein in general. The described method could be easily adapted for the specific and ultrasensitive immuno-PCR-based detection of traces of any food allergen that is currently being quantified with ELISA, which is of critical importance for people with food allergies. Full article

(This article belongs to the Special Issue Deciphering Allergies—Structural and Immunological Characterization of Allergenic Proteins and Immunomodulatory Agents)

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