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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
immunology and microbiology
Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin
Allergy: European Journal of Allergy and Clinical Immunology, Volume 75, No. 11, Year 2020
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Description
Background: Tropomyosins are highly conserved proteins, an attribute that forms the molecular basis for their IgE antibody cross-reactivity. Despite sequence similarities, their allergenicity varies greatly between ingested and inhaled invertebrate sources. In this study, we investigated the relationship between the structural stability of different tropomyosins, their endolysosomal degradation patterns, and T-cell reactivity. Methods: We investigated the differences between four tropomyosins—the major shrimp allergen Pen m 1 and the minor allergens Der p 10 (dust mite), Bla g 7 (cockroach), and Ani s 3 (fish parasite)—in terms of IgE binding, structural stability, endolysosomal degradation and subsequent peptide generation, and T-cell cross-reactivity in a BALB/c murine model. Results: Tropomyosins displayed different melting temperatures, which did not correlate with amino acid sequence similarities. Endolysosomal degradation experiments demonstrated differential proteolytic digestion, as a function of thermal stability, generating different peptide repertoires. Pen m 1 (Tm 42°C) and Der p 10 (Tm 44°C) elicited similar patterns of endolysosomal degradation, but not Bla g 7 (Tm 63°C) or Ani s 3 (Tm 33°C). Pen m 1–specific T-cell clones, with specificity for regions highly conserved in all four tropomyosins, proliferated weakly to Der p 10, but did not proliferate to Bla g 7 and Ani s 3, indicating lack of T-cell epitope cross-reactivity. Conclusions: Tropomyosin T-cell cross-reactivity, unlike IgE cross-reactivity, is dependent on structural stability rather than amino acid sequence similarity. These findings contribute to our understanding of cross-sensitization among different invertebrates and design of suitable T-cell peptide-based immunotherapies for shrimp and related allergies. © 2020 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd
Authors & Co-Authors
Kamath, Sandip D.
Australia, Townsville
James Cook University
Scheiblhofer, Sandra
Austria, Salzburg
Universität Salzburg
Taki, Aya C.
Australia, Melbourne
University of Melbourne
Ramsland, Paul A.
Australia, Melbourne
Rmit University
Thalhamer, Josef
Austria, Salzburg
Universität Salzburg
Rolland, Jennifer M.
Australia, Clayton
Monash University
Australia, Melbourne
The Alfred
O'Hehir, Robyn E.
Australia, Clayton
Monash University
Australia, Melbourne
The Alfred
Ferreira, Fátima D.
Austria, Salzburg
Universität Salzburg
Weiss, Richard
Austria, Salzburg
Universität Salzburg
Lopata, Andreas Ludwig
Australia, Townsville
James Cook University
Statistics
Citations: 21
Authors: 10
Affiliations: 8
Identifiers
Doi:
10.1111/all.14410
ISSN:
01054538