Cross-reactive epitopes and their role in food allergy

Kamath, Sandip D.; Bublin, Merima; Kitamura, Katsumasa; Matsui, Teruaki; Ito, Komei; Lopata, Andreas L.

doi:10.1016/j.jaci.2022.12.827

Cited by 30 publications

(20 citation statements)

References 157 publications

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“…Our findings demonstrate concomitant reactivity among these arginine kinase allergens, indicating shared immunological characteristics. The complexity of sensitization patterns associated with arginine kinase allergens is evident from our findings and other studies, 40 highlighting the need for further research.…”

Section: Discussionsupporting

confidence: 54%

“…39 We explored concomitant reactivity among arginine kinase MA's that have been identified as allergens in different arthropods, namely focusing on Pen m 2, Bla g 9 and Der p 20. 40 Our findings demonstrate concomitant reactivity among these arginine kinase allergens, indicating shared immunological characteristics. The complexity of sensitization patterns associated with arginine kinase allergens is evident from our findings and other studies, 40 highlighting the need for further research.…”

Section: Discussionmentioning

confidence: 51%

“…We explored concomitant reactivity among arginine kinase MA's that have been identified as allergens in different arthropods, namely focusing on Pen m 2, Bla g 9 and Der p 20 40 . Our findings demonstrate concomitant reactivity among these arginine kinase allergens, indicating shared immunological characteristics.…”

Section: Discussionmentioning

confidence: 84%

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Sensitization profiles to house dust mite Dermatophagoides pteronyssinus molecular allergens in the Lithuanian population: Understanding allergic sensitization patterns

Biliute,

Miskinyte,

Miskiniene

et al. 2024

Clinical & Translational All

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BackgroundHouse dust mite (HDM) allergy is a prevalent global health concern, with varying sensitization profiles observed across populations. We aimed to provide a comprehensive assessment of molecular allergen sensitization patterns in the Lithuanian population, with a focus on Dermatophagoides pteronyssinus (Der p), and investigate patterns of concomitant reactivity among different allergens to enhance the accuracy of HDM allergy diagnostics.MethodsA comprehensive analysis of 1520 patient test results in Lithuania from 2020 to 2022 was performed. Sensitization patterns to major (Der p 1, Der p 2, and Der p 23) and minor (Der p 5, Der p 7, and Der p 21) Der p allergen components were described using molecular‐based diagnostics. Additionally, we investigated sensitization to allergen components from other allergen sources, including tropomyosins (Der p 10, Per a 7, Pen m 1, Ani s 3, Blo t 10) and arginine kinases (Pen m 2, Bla g 9, Der p 20).ResultsThis study reveals a high prevalence of HDM sensitization in Lithuania ‐ 481 individuals (45.38% of the sensitized group) exhibited sensitization to at least one Der p allergen component. Importantly, within the sensitized group, 37.21% of patients were sensitized to Der p 5, Der p 7, or Der p 21 in addition to major allergenic components. Distinct sensitization patterns were observed across different age groups, indicating the influence of age‐related factors. Furthermore, we confirmed cross‐reactivity between Der p 5 and Blo t 5 as well as between Der p 21 and Blo t 21, emphasizing the clinical relevance of these associations. We also highlighted the complexity of sensitization patterns among tropomyosins and arginine kinases.ConclusionThis study provides valuable insights into HDM allergy sensitization profiles in Lithuania, emphasizing the importance of considering major and minor HDM allergen components for accurate diagnosis and management of HDM‐related allergic diseases. Differences between populations and age‐related factors impact sensitization patterns. Understanding concomitant reactivity among allergens, such as Der p 5 and Blo t 5, Der p 21 and Blo t 21, tropomyosins, and arginine kinases, is crucial for improving diagnostic strategies and developing targeted interventions for allergic individuals.

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Section: Discussionsupporting

confidence: 54%

Section: Discussionmentioning

confidence: 51%

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Sensitization profiles to house dust mite Dermatophagoides pteronyssinus molecular allergens in the Lithuanian population: Understanding allergic sensitization patterns

Biliute,

Miskinyte,

Miskiniene

et al. 2024

Clinical & Translational All

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“…Nevertheless, forecasting cross-reactivity between distantly related allergens remains a formidable challenge 42 . Allergen cross-reactivity typically occurs when IgE antibodies attach to either identical (with more than 70% sequence similarity) or closely resembling surface regions of another allergen that is related 26 , 28 . Less sequence identity or non-homologous allergens have not been comprehensively evaluated.…”

Section: Discussionmentioning

confidence: 99%

“…Many factors influence cross-reactivity, such as the immune response to the allergen in a host, the level of exposure to the allergen, and the type of allergen 27 . While numerous reports exist on IgE cross-reactivity among Hymenoptera venoms 28 , 29 , there is a lack of information concerning the potential cross-reaction between S. geminata and M. pilosula ant venom. Therefore, this study aims to predict cross-reactions among unrelated allergens from ant venoms using an in silico approach and assessing the cross-reactivity of recombinant Sol g proteins with M. pilosula -specific IgE via the immunoblotting method.…”

Section: Introductionmentioning

confidence: 99%

Structure-based epitope prediction and assessment of cross-reactivity of Myrmecia pilosula venom-specific IgE and recombinant Sol g proteins (Solenopsis geminata)

Buraphaka,

Dobutr,

Wiese

et al. 2024

Sci Rep

Self Cite

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The global distribution of tropical fire ants (Solenopsis geminata) raises concerns about anaphylaxis and serious medical issues in numerous countries. This investigation focused on the cross-reactivity of allergen-specific IgE antibodies between S. geminata and Myrmecia pilosula (Jack Jumper ant) venom proteins due to the potential emergence of cross-reactive allergies in the future. Antibody epitope analysis unveiled one predominant conformational epitope on Sol g 1.1 (PI score of 0.989), followed by Sol g 2.2, Sol g 4.1, and Sol g 3.1. Additionally, Pilosulin 1 showed high allergenic potential (PI score of 0.94), with Pilosulin 5a (PI score of 0.797) leading in B-cell epitopes. The sequence analysis indicated that Sol g 2.2 and Sol g 4.1 pose a high risk of cross-reactivity with Pilosulins 4.1a and 5a. Furthermore, the cross-reactivity of recombinant Sol g proteins with M. pilosula-specific IgE antibodies from 41 patients revealed high cross-reactivity for r-Sol g 3.1 (58.53%) and r-Sol g 4.1 (43.90%), followed by r-Sol g 2.2 (26.82%), and r-Sol g 1.1 (9.75%). Therefore, this study demonstrates cross-reactivity (85.36%) between S. geminata and M. pilosula, highlighting the allergenic risk. Understanding these reactions is vital for the prevention of severe allergic reactions, especially in individuals with pre-existing Jumper Jack ant allergy, informing future management strategies.

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The Allergen Profile of Two Edible Insect Species—Acheta domesticus and Hermetia illucens

Karnaneedi,

Johnston,

Bose

et al. 2024

Molecular Nutrition Food Res

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ScopeEdible insect proteins are increasingly introduced as an alternative sustainable food source to address the world's need to feed the growing population. Tropomyosin is the main insect allergen; however, additional potential allergens are not well characterized and the impact of extraction procedures on immunological reactivity is unknown.Methods and resultsProteins from different commercial food products derived from cricket (Acheta domesticus) and black soldier fly (BSF) (Hermetia illucens) are extracted using five different extraction buffers. The proteins are analyzed by SDS‐PAGE and immunoblotting using allergen‐specific antibodies and crustacean allergic patient sera. IgE binding bands are analyzed by mass spectrometry as well as the complete allergen profile of all 30 extracts. Urea‐based buffers are most efficient in extracting insect allergens. Shrimp‐specific antibody cross‐reactivity to tropomyosin from cricket and BSF indicates high sequence and structural similarity between shrimp and insects. Additional unique allergens are identified in both species, including hemocyanin, vitellogenin, HSP20, apolipophorin‐III, and chitin‐binding protein.ConclusionsIdentifying potential allergenic proteins and their isoforms in cricket and BSF requires specific extraction approaches using urea‐based methods. While tropomyosin is the most abundant and immunoreactive allergen, seven unique allergens are identified, highlighting the need for insect species‐specific allergen detection in food products.

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Cross-reactive epitopes and their role in food allergy

Cited by 30 publications

References 157 publications

Sensitization profiles to house dust mite Dermatophagoides pteronyssinus molecular allergens in the Lithuanian population: Understanding allergic sensitization patterns

Sensitization profiles to house dust mite Dermatophagoides pteronyssinus molecular allergens in the Lithuanian population: Understanding allergic sensitization patterns

Structure-based epitope prediction and assessment of cross-reactivity of Myrmecia pilosula venom-specific IgE and recombinant Sol g proteins (Solenopsis geminata)

The Allergen Profile of Two Edible Insect Species—Acheta domesticus and Hermetia illucens

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