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Glycoproteins generated by engineering bacterial glycosylation machineries have been proposed to be a viable alternative to traditional conjugation methods.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>In this work we expressed the <jats:italic>C. jejuni<\/jats:italic> oligosaccharyltansferase (OTase) PglB, responsible for <jats:italic>N<\/jats:italic>-linked protein glycosylation together with a suitable acceptor protein (AcrA) in <jats:italic>Yersinia enterocolitica<\/jats:italic> O9 cells. MS analysis of the acceptor protein demonstrated the transfer of a polymer of N-formylperosamine to AcrA <jats:italic>in vivo<\/jats:italic>. Because <jats:italic>Y. enterocolitica<\/jats:italic> O9 and <jats:italic>Brucella abortus<\/jats:italic> share an identical O polysaccharide structure, we explored the application of the resulting glycoprotein in vaccinology and diagnostics of brucellosis, one of the most common zoonotic diseases with over half a million new cases annually. Injection of the glycoprotein into mice generated an IgG response that recognized the O antigen of <jats:italic>Brucella<\/jats:italic>, although this response was not protective against a challenge with a virulent <jats:italic>B. abortus<\/jats:italic> strain. The recombinant glycoprotein coated onto magnetic beads was efficient in differentiating between na\u00efve and infected bovine sera.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion<\/jats:title>\n            <jats:p>Bacterial engineered glycoproteins show promising applications for the development on an array of diagnostics and immunoprotective opportunities in the future.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1475-2859-11-13","type":"journal-article","created":{"date-parts":[[2012,1,25]],"date-time":"2012-01-25T19:23:56Z","timestamp":1327519436000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":65,"title":["Exploiting the Campylobacter jejuni protein glycosylation system for glycoengineering vaccines and diagnostic tools directed against brucellosis"],"prefix":"10.1186","volume":"11","author":[{"given":"Jeremy A","family":"Iwashkiw","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Messele A","family":"Fentabil","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amirreza","family":"Faridmoayer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dominic C","family":"Mills","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark","family":"Peppler","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cecilia","family":"Czibener","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andres E","family":"Ciocchini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Diego J","family":"Comerci","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Juan E","family":"Ugalde","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mario F","family":"Feldman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2012,1,25]]},"reference":[{"issue":"19-20","key":"644_CR1","doi-asserted-by":"publisher","first-page":"2229","DOI":"10.1007\/s00018-006-6311-4","volume":"63","author":"G Pappas","year":"2006","unstructured":"Pappas G, Panagopoulou P, Christou L, Akritidis N: Brucella as a biological weapon. 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