2017
DOI: 10.1016/j.jaip.2017.02.015
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Identification of the larval serum proteins as major fruit fly (Drosophila melanogaster) occupational allergens

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Cited by 5 publications
(7 citation statements)
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“…Hopefully, a few insect allergens have been characterized as rather specific for (edible) insects since they primarily occur in insects and are much less abundant or lacking in other organisms phylogenetically-related to insects. These specific insect allergens essentially correspond to proteins dedicated to the recognition of environmental chemical signals, such as the chemosensory proteins and the odorant-or pheromone-binding proteins [73], Bla g 3 from the German cockroach (Blattella germanica) [74], and Per a 3 from the American cockroach (Periplaneta americana) [75], hexamerin from the edible cricket Gryllus bimaculatus [76], hexamerin from the maggot fly Caliphora erythrocephala [77], hexamerin from the fruit fly Drosophila melanogaster [78], and hexamerin from the yellow mealworm Tenebrio molitor [79]. Except for CSP and OBP, which usually are poorly glycosylated, other specific allergens of insects contain N-glycosylation sites and apparently consist of glycosylated proteins.…”
Section: Discussionmentioning
confidence: 99%
“…Hopefully, a few insect allergens have been characterized as rather specific for (edible) insects since they primarily occur in insects and are much less abundant or lacking in other organisms phylogenetically-related to insects. These specific insect allergens essentially correspond to proteins dedicated to the recognition of environmental chemical signals, such as the chemosensory proteins and the odorant-or pheromone-binding proteins [73], Bla g 3 from the German cockroach (Blattella germanica) [74], and Per a 3 from the American cockroach (Periplaneta americana) [75], hexamerin from the edible cricket Gryllus bimaculatus [76], hexamerin from the maggot fly Caliphora erythrocephala [77], hexamerin from the fruit fly Drosophila melanogaster [78], and hexamerin from the yellow mealworm Tenebrio molitor [79]. Except for CSP and OBP, which usually are poorly glycosylated, other specific allergens of insects contain N-glycosylation sites and apparently consist of glycosylated proteins.…”
Section: Discussionmentioning
confidence: 99%
“…Tropomyosin and hexamerin LSP‐2 corresponded to allergens previously described in D . melanogaster 5 …”
Section: Figurementioning
confidence: 99%
“…It has also become an important allergen source in laboratory environments with sensitization rates between 6% and 31% in laboratory workers. 2,3 Different proteins have been identified as presumable D. melanogaster allergens, 4,5 and three are included in Allergome database (www.aller gome.org) tropomyosin, arginine kinase and Mn superoxide dismutase. All of them were identified by indirect methods, not in patients sensitized to D. melanogaster.…”
Section: Drosophila Melanogastermentioning
confidence: 99%
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