biostudies-literatureUzulmez OAmt der NÖ LandesregierungAustrian Science Fund FWF723363https://www.ebi.ac.uk/biostudies/studies/S-EPMC8522509biostudies-literatureUnknown12Peanut 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^OHS 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 perfoFrontiers in plant scienceThe 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.PMC8522509P 30936-B30P 30936Breiteneder HLengger NMayr VKalic THemmer WUzulmez ORadauer CHafner CTscheppe AfalseThe 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.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^OHS 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 perfo2021-01-01T00:00:00Z20212026-05-09T09:38:37.264Z2024-11-07T01:12:57.387ZS-EPMC85225093467137210.3389/fpls.2021.723363