{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,6]],"date-time":"2025-11-06T20:01:28Z","timestamp":1762459288560,"version":"3.40.4"},"reference-count":33,"publisher":"S. Karger AG","issue":"2","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"},{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int Arch Allergy Immunol"],"published-print":{"date-parts":[[2015]]},"abstract":"<b><i>Background:<\/i><\/b> The incidence of Amaranthaceae pollen allergy has increased due to the desertification occurring in many countries. In some regions of Spain, <i>Salsola kali <\/i>is the main cause of pollinosis, at almost the same level as olive and grass pollen. Sal k 1 - the sensitization marker of <i>S. kali <\/i>pollinosis - is used in clinical diagnosis, but is purified at a low yield from pollen. We aimed to produce a recombinant (r)Sal k 1 able to span the structural and immunological properties of the natural isoforms from pollen, and validate its potential use for diagnosis. <b><i>Methods:<\/i><\/b> Specific cDNA was amplified by PCR, cloned into the pET41b vector and used to transform BL21 (DE3) <i>Escherichia coli <\/i>cells. Immunoblotting, ELISA, basophil activation and skin-prick tests were used to validate the recombinant protein against Sal k 1 isolated from pollen. Sera and blood cells from <i>S. kali <\/i>pollen-sensitized patients and specific monoclonal and polyclonal antisera were used. <b><i>Results:<\/i><\/b> rSal k 1 was produced in bacteria with a yield of 7.5 mg\/l of cell culture. The protein was purified to homogeneity and structural and immunologically validated against the natural form. rSal k 1 exhibited a higher IgE cross-reactivity with plant-derived food extracts such as peanut, almond or tomato than with pollen sources such as <i>Platanus acerifolia<\/i> and Oleaceae members. <b><i>Conclusions:<\/i><\/b> rSal k 1 expressed in bacteria retains intact structural and immunological properties in comparison to the pollen-derived allergen. It spans the immunological properties of most of the isoforms found in pollen, and it might substitute natural Sal k 1 in clinical diagnosis.<\/jats:p>","DOI":"10.1159\/000434680","type":"journal-article","created":{"date-parts":[[2015,7,21]],"date-time":"2015-07-21T21:02:47Z","timestamp":1437512567000},"page":"83-93","source":"Crossref","is-referenced-by-count":12,"title":["A Recombinant Sal k 1 Isoform as an Alternative to the Polymorphic Allergen from <b><i>Salsola kali<\/i><\/b> Pollen for Allergy Diagnosis"],"prefix":"10.1159","volume":"167","author":[{"given":"Salvador","family":"Mas","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patrice","family":"Boissy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rafael 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