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Sarcoplasmic calcium‐binding protein and alcohol dehydrogenase, new occupational allergens in the fruit fly Drosophila melanogaster.

Authors :
Betancor, Diana
López‐Matas, María A.
González‐Ruiz, Azahara
Martín‐López, Laura
Carnés, Jerónimo
Fernández‐Nieto, Maria del Mar
Source :
Clinical & Experimental Allergy. Oct2021, Vol. 51 Issue 10, p1387-1390. 4p. 1 Black and White Photograph, 1 Chart.
Publication Year :
2021

Abstract

The only I D i . I melanogaster i allergen confirmed until now is LSP-2 (hexamerin),5 and however, the identification of this allergen was only shown by comparing the IgE immunoblot band pattern with the biding profile of an anti-LSP-2 antibody. This protein is a relevant allergen described in Crustacea.7 Although patient did not refer allergic symptoms after eating shellfish, sensitization was not determined because she refused a prick-by-prick test with shrimp. Only two ADHs have been described as allergens to date, both from fungi; Cand a 1, in I Candida albicans i 9 and Cur l ADH in I Curvularia lunata i .10 ADHs are glycolytic enzymes involved in NAD+regeneration and in the I D i . Keywords: allergens and epitopesss; IgE; occupational allergies; rhinitis EN allergens and epitopesss IgE occupational allergies rhinitis 1387 1390 4 10/01/21 20211001 NES 211001 Key Messages We reported a case of occupational allergy to I Drosophila melanogaster i mediated by four allergens. [Extracted from the article]

Details

Language :
English
ISSN :
09547894
Volume :
51
Issue :
10
Database :
Academic Search Index
Journal :
Clinical & Experimental Allergy
Publication Type :
Academic Journal
Accession number :
152707600
Full Text :
https://doi.org/10.1111/cea.13901