{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T10:55:42Z","timestamp":1768560942232,"version":"3.49.0"},"reference-count":24,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2002,8,19]],"date-time":"2002-08-19T00:00:00Z","timestamp":1029715200000},"content-version":"vor","delay-in-days":18,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Clin Experimental Allergy"],"published-print":{"date-parts":[[2002,8]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p><jats:bold>Background<\/jats:bold> Tropomyosin belongs to a class of highly conserved proteins in invertebrates and vertebrates. The invertebrate tropomyosins are allergenic in man with high IgE cross\u2010reactivity and have been therefore referred to as pan\u2010allergens.<\/jats:p><jats:p><jats:bold>Objectives<\/jats:bold> This study aimed to clone and identify the IgE epitopes of tropomyosin from <jats:italic>Blomia tropicalis<\/jats:italic> (Blo t 10) mite. Cross\u2010reactivity between the IgE epitopes of Blo t 10 and Der p 10 was also evaluated.<\/jats:p><jats:p><jats:bold>Methods<\/jats:bold> Blo t 10 was isolated using mouse anti\u2010Der p 10 antibodies. Allergenicity of the cloned Blo t 10 was confirmed by skin prick test (SPT) and enzyme\u2010linked immunosorbent assay (ELISA). Dose\u2010dependent inhibition assay was performed to determine the degree of IgE cross\u2010reactivity between Blo t 10 and Der p 10. Overlapping polymerase chain reaction\u2010derived cDNA were generated and expressed as glutathione\u2010S\u2010transferase (GST) recombinant proteins in <jats:italic>Escherichia coli<\/jats:italic> and used to identify shared and unique IgE epitopes of Blo t 10 and Der p 10.<\/jats:p><jats:p><jats:bold>Results<\/jats:bold> The cloned Blo t 10 shared up to 96% amino acid identity to tropomyosin of other mites. SPT and ELISA IgE\u2010immunoassay showed recombinant Blo t 10 sensitization rates of between 20% and 29% in atopic subjects. Results of SPT and dose\u2010dependent inhibition assays showed that some allergic individuals had unique IgE epitopes for Blo t 10. IgE epitope mapping of Blo t 10 revealed that the epitopes were mainly located at N\u2010 and C\u2010termini of the molecule. The results of ELISA inhibition assays of overlapping recombinant fragments indicated that the unique IgE epitopes of Blo t 10 were located at the C\u2010terminal.<\/jats:p><jats:p><jats:bold>Conclusion<\/jats:bold> Although Blo t 10 and Der p 10 are highly conserved (shared 95% amino acids identity) and significantly cross\u2010reactive, unique IgE epitopes do exist. The results suggest the potential deficiency of using only one of these highly conserved allergens as diagnostic or therapeutic reagents.<\/jats:p>","DOI":"10.1046\/j.1365-2745.2002.01449.x","type":"journal-article","created":{"date-parts":[[2003,3,11]],"date-time":"2003-03-11T09:52:52Z","timestamp":1047376372000},"page":"1203-1210","source":"Crossref","is-referenced-by-count":57,"title":["Identification of shared and unique immunoglobulin E\u00a0epitopes of the highly conserved tropomyosins in <i>Blomia tropicalis<\/i> and <i>Dermatophagoides pteronyssinus<\/i>"],"prefix":"10.1111","volume":"32","author":[{"given":"F. 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