{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Roth-Walter F"],"funding":["Austrian Science Fund FWF"],"pagination":["17416-21"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4067174"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["289(25)"],"pubmed_abstract":["It is hypothesized that allergens are at the borderline of self and non-self and, through as yet elusive circumstances, mount a Th2 response for allergic sensitization. The major birch pollen allergen Bet v 1 is considered the prototype for the PR-10 protein family causing respiratory allergy. Here, we give structural evidence that Bet v 1 is a lipocalin-like protein with a striking structural resemblance to human lipocalin 2. Lipocalin 2 is highly expressed in the lung where it exerts immunoregulatory functions dependent on being loaded with siderophore-bound iron (holo-form) or not (apo-form). We demonstrate that similar to lipocalin 2, Bet v 1 is capable of binding iron via catechol-based siderophores. Thereby, calculated Kd values of 66 nm surpassed affinities to known ligands nearly b"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Bet v 1 from birch pollen is a lipocalin-like protein acting as allergen only when devoid of iron by promoting Th2 lymphocytes."],"pmcid":["PMC4067174"],"funding_grant_id":["F 4606"],"pubmed_authors":["Mothes-Luksch N","Roth GA","Pacios LF","Jensen-Jarolim E","Singer J","Gomez-Casado C","Roth-Walter F","Diaz-Perales A"],"additional_accession":[]},"is_claimable":false,"name":"Bet v 1 from birch pollen is a lipocalin-like protein acting as allergen only when devoid of iron by promoting Th2 lymphocytes.","description":"It is hypothesized that allergens are at the borderline of self and non-self and, through as yet elusive circumstances, mount a Th2 response for allergic sensitization. The major birch pollen allergen Bet v 1 is considered the prototype for the PR-10 protein family causing respiratory allergy. Here, we give structural evidence that Bet v 1 is a lipocalin-like protein with a striking structural resemblance to human lipocalin 2. Lipocalin 2 is highly expressed in the lung where it exerts immunoregulatory functions dependent on being loaded with siderophore-bound iron (holo-form) or not (apo-form). We demonstrate that similar to lipocalin 2, Bet v 1 is capable of binding iron via catechol-based siderophores. Thereby, calculated Kd values of 66 nm surpassed affinities to known ligands nearly b","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jun","modification":"2025-04-18T12:39:11.595Z","creation":"2019-03-27T01:30:41Z"},"accession":"S-EPMC4067174","cross_references":{"pubmed":["24798325"],"doi":["10.1074/jbc.M114.567875"]}}