{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T04:02:56Z","timestamp":1780545776036,"version":"3.54.1"},"reference-count":34,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T00:00:00Z","timestamp":1772928000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T00:00:00Z","timestamp":1772928000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100002428","name":"Austrian Science Fund","doi-asserted-by":"publisher","award":["I 5640\u2010N"],"award-info":[{"award-number":["I 5640\u2010N"]}],"id":[{"id":"10.13039\/501100002428","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Biotech &amp; Bioengineering"],"published-print":{"date-parts":[[2026,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Secretory immunoglobulin A (sIgA) is a promising emerging biopharmaceutical candidate, but it currently lacks a standardized platform for purification. To address this, a novel affinity chromatography resin was developed by immobilizing protein variants of the\n                    <jats:italic>Streptococcus pneumoniae<\/jats:italic>\n                    surface protein, SpsA, as an affinity ligand. SpsA targets the secretory component of sIgA, which increases selectivity and minimizes co\u2010purification of product\u2010related impurities. Directed attachment between a single cysteine residue and macroporous epoxy\u2010activated supports was employed as an immobilization strategy. Ligand orientation on the resin surface is of utmost importance, as the initial SpsA variant was unable to bind sIgA after immobilization. The cysteine residue was subsequently relocated from the C\u2010terminus to either the N\u2010terminus or loop region of the ligand, resulting in a functional resin. 177\u2009nmol SpsA\/mL resin were immobilized on the agarose\u2010based resin, resulting in an equilibrium binding capacity of 9.1\u2009mg sIgA\/mL resin. SpsA resin was able to selectively purify sIgA from cell culture supernatant under dynamic conditions with free secretory component as the only product\u2010related impurity. SpsA\u2010based affinity chromatography may enable a scalable purification process for sIgA through an appropriate resin structure and improved selectivity.\n                  <\/jats:p>","DOI":"10.1002\/bit.70189","type":"journal-article","created":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T06:12:22Z","timestamp":1773036742000},"page":"1531-1543","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Engineered Bacterial Ligand From\n                    <i>Streptococcus pneumoniae<\/i>\n                    on Macroporous Resins for Selective Affinity Capture of Secretory IgA"],"prefix":"10.1002","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7312-3250","authenticated-orcid":false,"given":"David","family":"Scheich","sequence":"first","affiliation":[{"name":"Department of Biotechnology and Food Science, Institute of Bioprocess Science and Engineering BOKU University Vienna 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