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Group 10 Allergens (Tropomyosins) from House-Dust Mites May Cause Covariation of Sensitization to Allergens from Other Invertebrates

Shafique, Rubaba Hamid, Inam, Muhammad, Ismail, Muhammad, Chaudhary, Farhana Riaz·2012·Allergy & Rhinology

Abstract

Group 10 allergens (tropomyosins) have been assumed to be a major cause of cross-reactivity between house-dust mites (HDMs) and other invertebrates. Despite all of the published data regarding the epidemiology, percent IgE binding and level of sensitization in the population, the role of tropomyosin as a cross-reactive allergen in patients with multiple allergy syndrome still remains to be elucidated. Homology between amino acid sequences reported in allergen databases of selected invertebrate tropomyosins was determined with Der f 10 as the reference allergen. The 66.9 and 54.4% identities were found with selected crustacean and insect species, respectively, whereas only 20.4% identity was seen with mollusks. A similar analysis was performed using reported B-cell IgE-binding epitopes from Met e1 (shrimp allergen) and Bla g7 (cockroach allergen) with other invertebrate tropomyosins. The percent identity in linear sequences was higher than 35% in mites, crustaceans, and cockroaches. The polar and hydrophobic regions in these groups were highly conserved. These findings suggest that tropomyosin may be a major cause of covariation of sensitization between HDMs, crustaceans, and some species of insects and mollusks.

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Figure 1. Amino acid sequence alignment: comparison of Der f 10 allergen with major group 10 allergens from mite species using the clustalo algorithm. With 240 identical (*), 26 conserved (:) and 6 semiconserved (.) positions the identity is 84.2% (UniProt FASTA). For abbreviations refer to Appendix A.
Figure 1. Amino acid sequence alignment: comparison of Der f 10 allergen with major group 10 allergens from mite species using the clustalo algorithm. With 240 identical (*), 26 conserved (:) and 6 semiconserved (.) positions the identity is 84.2% (UniProt FASTA). For abbreviations refer to Appendix A.CC BY-NC-ND · PubMed Central
Figure 2. Phylogenetic tree based on aligned tropomyosin proteins from invertebrates.103 For abbreviations, see Appendix A.
Figure 2. Phylogenetic tree based on aligned tropomyosin proteins from invertebrates.103 For abbreviations, see Appendix A.CC BY-NC-ND · PubMed Central
Figure 3. Amino acid sequence alignment: comparison of Der f 10 and Der p 10 allergens with major tropomyosin allergens from crustacean species using the clustalo algorithm. With 190 identical (*), 37 conserved (:), and 7 semiconserved (.) positions the identity is 66.9% (UniProt FASTA). For abbreviations, see Appendix A.
Figure 3. Amino acid sequence alignment: comparison of Der f 10 and Der p 10 allergens with major tropomyosin allergens from crustacean species using the clustalo algorithm. With 190 identical (*), 37 conserved (:), and 7 semiconserved (.) positions the identity is 66.9% (UniProt FASTA). For abbreviations, see Appendix A.CC BY-NC-ND · PubMed Central
Figure 4. Amino acid sequence alignment: comparison of Der f 10 and Der p 10 allergens with major tropomyosin allergens from insect species using the clustalo algorithm. With 155 identical (*), 60 conserved (:), and 16 semiconserved (.) positions the identity is 54.4% (UniProt FASTA). For abbreviations, see Appendix A.
Figure 4. Amino acid sequence alignment: comparison of Der f 10 and Der p 10 allergens with major tropomyosin allergens from insect species using the clustalo algorithm. With 155 identical (*), 60 conserved (:), and 16 semiconserved (.) positions the identity is 54.4% (UniProt FASTA). For abbreviations, see Appendix A.CC BY-NC-ND · PubMed Central
Figure 5. Amino acid sequence alignment: comparison of Der f 10 and Der p 10 allergens with major tropomyosin allergens from mollusk species using the clustalo algorithm. With 58 identical (*), 36 conserved (:), and 7 semiconserved (.) positions the identity is 20.4% (UniProt FASTA). For abbreviations, see Appendix A.
Figure 5. Amino acid sequence alignment: comparison of Der f 10 and Der p 10 allergens with major tropomyosin allergens from mollusk species using the clustalo algorithm. With 58 identical (*), 36 conserved (:), and 7 semiconserved (.) positions the identity is 20.4% (UniProt FASTA). For abbreviations, see Appendix A.CC BY-NC-ND · PubMed Central
Figure 6. IgE-binding epitope (peptide 1, 47–63, and peptide 2, 150–158) from Met e 1 aligned with species of invertebrates (a, mites; b, crustacea; c, mollusks; and d, insects). Conserved polar regions have been highlighted (UniProt FASTA). For abbreviations, see Appendix A.
Figure 6. IgE-binding epitope (peptide 1, 47–63, and peptide 2, 150–158) from Met e 1 aligned with species of invertebrates (a, mites; b, crustacea; c, mollusks; and d, insects). Conserved polar regions have been highlighted (UniProt FASTA). For abbreviations, see Appendix A.CC BY-NC-ND · PubMed Central
Figure 7. Analysis of IgE-binding epitopes of Bla g 7 (Blatella germanica tropomyosin) with selected invertebrate species. Conserved polar regions have been highlighted (UniProt FASTA). For abbreviations, see Appendix A.
Figure 7. Analysis of IgE-binding epitopes of Bla g 7 (Blatella germanica tropomyosin) with selected invertebrate species. Conserved polar regions have been highlighted (UniProt FASTA). For abbreviations, see Appendix A.CC BY-NC-ND · PubMed Central

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Metadata

Authors
Shafique, R. H., Inam, M., Ismail, M., & Chaudhary, F. R.
Venue
Allergy & Rhinology
Published
2012-01
Volume
3
Issue
2
ISSN
  • 2152-6575
  • 2152-6567
Cited by
39
References
0
Language
en

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CoChat. (2026). Citation check: Group 10 Allergens (Tropomyosins) from House-Dust Mites May Cause Covariation of Sensitization to Allergens from Other Invertebrates. https://app.cochat.ai/papers/10.2500/ar.2012.3.0036
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Shafique, R. H., Inam, M., Ismail, M., & Chaudhary, F. R. (2012). Group 10 Allergens (Tropomyosins) from House-Dust Mites May Cause Covariation of Sensitization to Allergens from Other Invertebrates. Allergy & Rhinology. https://doi.org/10.2500/ar.2012.3.0036