<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>291(34)</volume><submitter>Sircar G</submitter><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>18016-29</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5016188</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Epitope Mapping of Rhi o 1 and Generation of a Hypoallergenic Variant: A CANDIDATE MOLECULE FOR FUNGAL ALLERGY VACCINES.</pubmed_title><pmcid>PMC5016188</pmcid><pubmed_authors>Saha S</pubmed_authors><pubmed_authors>Jana K</pubmed_authors><pubmed_authors>Sircar G</pubmed_authors><pubmed_authors>Gupta Bhattacharya S</pubmed_authors><pubmed_authors>Dasgupta A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Epitope Mapping of Rhi o 1 and Generation of a Hypoallergenic Variant: A CANDIDATE MOLECULE FOR FUNGAL ALLERGY VACCINES.</name><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</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Aug</publication><modification>2025-04-21T16:36:41.778Z</modification><creation>2019-03-27T02:23:49Z</creation></dates><accession>S-EPMC5016188</accession><cross_references><pubmed>27358405</pubmed><doi>10.1074/jbc.M116.732032</doi><doi>10.1074/jbc.m116.732032</doi></cross_references></HashMap>