{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Eichhorn S"],"funding":["FP7 Health"],"pagination":["e1900336"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6790652"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["63(18)"],"pubmed_abstract":["Scope
Allergies to lipid transfer proteins involve severe adverse reactions; thus, effective and sustainable therapies are desired. Previous attempts disrupting disulfide bonds failed to maintain immunogenicity; thus, the aim is to design novel hypoallergenic Pru p 3 variants and evaluate the applicability for treatment of peach allergy.Methods and results
Pru p 3 proline variant (PV) designed using in silico mutagenesis, cysteine variant (CV), and wild-type Pru p 3 (WT) are purified from Escherichia coli. Variants display homogenous and stable protein conformations with an altered secondary structure in circular dichroism. PV shows enhanced long-term storage capacities compared to CV similar to the highly stable WT. Using sera of 33 peach allergic patients, IgE-binding activity is reduced by 97% (PV) and 71% (CV) compared to WT. Both molecules show strong hypoallergenicity in Pru p 3 ImmunoCAP cross-inhibition and histamine release assays. Immunogenicity of PV is demonstrated with a phosphate-based adjuvant formulation in a mouse model.Conclusions
An in silico approach is used to generate a PV without targeting disulfide bonds, T cell epitopes, or previously reported IgE epitopes of Pru p 3. PV is strongly hypoallergenic while structurally stable and immunogenic, thus representing a promising candidate for peach allergen immunotherapy."],"journal":["Molecular nutrition & food research"],"pubmed_title":["Rational Design, Structure-Activity Relationship, and Immunogenicity of Hypoallergenic Pru p 3 Variants."],"pmcid":["PMC6790652"],"funding_grant_id":["FAST – Food Allergy Specific Immunotherapy (201871"],"pubmed_authors":["Papadopoulos NG","Laimer J","Asturias JA","Jensen BM","Portoles A","Lackner P","Ferreira F","Rigby N","Poulsen LK","Versteeg SA","Pablos I","Briza P","Gadermaier G","Fernandez-Rivas M","Horschlager A","Jongejan L","Steiner M","Eichhorn S","Mari A","van Ree R"],"additional_accession":[]},"is_claimable":false,"name":"Rational Design, Structure-Activity Relationship, and Immunogenicity of Hypoallergenic Pru p 3 Variants.","description":"Scope
Allergies to lipid transfer proteins involve severe adverse reactions; thus, effective and sustainable therapies are desired. Previous attempts disrupting disulfide bonds failed to maintain immunogenicity; thus, the aim is to design novel hypoallergenic Pru p 3 variants and evaluate the applicability for treatment of peach allergy.Methods and results
Pru p 3 proline variant (PV) designed using in silico mutagenesis, cysteine variant (CV), and wild-type Pru p 3 (WT) are purified from Escherichia coli. Variants display homogenous and stable protein conformations with an altered secondary structure in circular dichroism. PV shows enhanced long-term storage capacities compared to CV similar to the highly stable WT. Using sera of 33 peach allergic patients, IgE-binding activity is reduced by 97% (PV) and 71% (CV) compared to WT. Both molecules show strong hypoallergenicity in Pru p 3 ImmunoCAP cross-inhibition and histamine release assays. Immunogenicity of PV is demonstrated with a phosphate-based adjuvant formulation in a mouse model.Conclusions
An in silico approach is used to generate a PV without targeting disulfide bonds, T cell epitopes, or previously reported IgE epitopes of Pru p 3. PV is strongly hypoallergenic while structurally stable and immunogenic, thus representing a promising candidate for peach allergen immunotherapy.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Sep","modification":"2024-11-09T17:38:32.742Z","creation":"2019-10-30T08:21:27Z"},"accession":"S-EPMC6790652","cross_references":{"pubmed":["31207117"],"doi":["10.1002/mnfr.201900336"]}}