{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Uzulmez O"],"funding":["Amt der NÖ Landesregierung","Austrian Science Fund FWF"],"pagination":["723363"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8522509"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12"],"pubmed_abstract":["Peanut allergy is a potentially life-threatening disease that is mediated by allergen-specific immunoglobulin E (IgE) antibodies. The major peanut allergen Ara h 2, a 2S albumin seed storage protein, is one of the most dangerous and potent plant allergens. Ara h 2 is posttranslationally modified to harbor four disulfide bridges and three hydroxyprolines. These hydroxyproline residues are required for optimal IgE-binding to the DPYSP<sup>OH</sup>S motifs representing an immunodominant IgE epitope. So far, recombinant Ara h 2 has been produced in <i>Escherichia coli, Lactococcus lactis, Trichoplusia ni</i> insect cell, and <i>Chlamydomonas reinhardtii</i> chloroplast expression systems, which were all incapable of proline hydroxylation. However, molecular diagnosis of peanut allergy is perfo"],"journal":["Frontiers in plant science"],"pubmed_title":["The Major Peanut Allergen Ara h 2 Produced in &lt;i&gt;Nicotiana benthamiana&lt;/i&gt; Contains Hydroxyprolines and Is a Viable Alternative to the &lt;i&gt;E. Coli&lt;/i&gt; Product in Allergy Diagnosis."],"pmcid":["PMC8522509"],"funding_grant_id":["P 30936-B30","P 30936"],"pubmed_authors":["Breiteneder H","Lengger N","Mayr V","Kalic T","Hemmer W","Uzulmez O","Radauer C","Hafner C","Tscheppe A"],"additional_accession":[]},"is_claimable":false,"name":"The Major Peanut Allergen Ara h 2 Produced in &lt;i&gt;Nicotiana benthamiana&lt;/i&gt; Contains Hydroxyprolines and Is a Viable Alternative to the &lt;i&gt;E. Coli&lt;/i&gt; Product in Allergy Diagnosis.","description":"Peanut allergy is a potentially life-threatening disease that is mediated by allergen-specific immunoglobulin E (IgE) antibodies. The major peanut allergen Ara h 2, a 2S albumin seed storage protein, is one of the most dangerous and potent plant allergens. Ara h 2 is posttranslationally modified to harbor four disulfide bridges and three hydroxyprolines. These hydroxyproline residues are required for optimal IgE-binding to the DPYSP<sup>OH</sup>S motifs representing an immunodominant IgE epitope. So far, recombinant Ara h 2 has been produced in <i>Escherichia coli, Lactococcus lactis, Trichoplusia ni</i> insect cell, and <i>Chlamydomonas reinhardtii</i> chloroplast expression systems, which were all incapable of proline hydroxylation. However, molecular diagnosis of peanut allergy is perfo","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021","modification":"2026-05-09T09:38:37.264Z","creation":"2024-11-07T01:12:57.387Z"},"accession":"S-EPMC8522509","cross_references":{"pubmed":["34671372"],"doi":["10.3389/fpls.2021.723363"]}}