{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["291(34)"],"submitter":["Sircar G"],"pubmed_abstract":["Efficacy of allergen-specific immunotherapy is often severely impaired by detrimental IgE-mediated side effects of native allergen during vaccination. Here, we present the molecular determinants for IgE recognition of Rhi o 1 and eventually converting the allergen into a hypoallergenic immunogen to restrain health hazards during desensitization. Rhi o 1 is a respiratory fungal allergen. Despite having cross-reactivity with cockroach allergen, we observed that non-cross-reactive epitope predominantly determined IgE binding to Rhi o 1. Denaturation and refolding behavior of the allergen confirmed that its IgE reactivity was not essentially conformation-dependent. A combinatorial approach consisting of computational prediction and a peptide-based immunoassay identified two peptides ((44)TGEYL"],"journal":["The Journal of biological chemistry"],"pagination":["18016-29"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5016188"],"repository":["biostudies-literature"],"pubmed_title":["Epitope Mapping of Rhi o 1 and Generation of a Hypoallergenic Variant: A CANDIDATE MOLECULE FOR FUNGAL ALLERGY VACCINES."],"pmcid":["PMC5016188"],"pubmed_authors":["Saha S","Jana K","Sircar G","Gupta Bhattacharya S","Dasgupta A"],"additional_accession":[]},"is_claimable":false,"name":"Epitope Mapping of Rhi o 1 and Generation of a Hypoallergenic Variant: A CANDIDATE MOLECULE FOR FUNGAL ALLERGY VACCINES.","description":"Efficacy of allergen-specific immunotherapy is often severely impaired by detrimental IgE-mediated side effects of native allergen during vaccination. Here, we present the molecular determinants for IgE recognition of Rhi o 1 and eventually converting the allergen into a hypoallergenic immunogen to restrain health hazards during desensitization. Rhi o 1 is a respiratory fungal allergen. Despite having cross-reactivity with cockroach allergen, we observed that non-cross-reactive epitope predominantly determined IgE binding to Rhi o 1. Denaturation and refolding behavior of the allergen confirmed that its IgE reactivity was not essentially conformation-dependent. A combinatorial approach consisting of computational prediction and a peptide-based immunoassay identified two peptides ((44)TGEYL","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Aug","modification":"2025-04-21T16:36:41.778Z","creation":"2019-03-27T02:23:49Z"},"accession":"S-EPMC5016188","cross_references":{"pubmed":["27358405"],"doi":["10.1074/jbc.M116.732032","10.1074/jbc.m116.732032"]}}