{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T11:45:34Z","timestamp":1791287134674,"version":"4.1.0"},"reference-count":41,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            In\n            <jats:italic>Campylobacter jejuni<\/jats:italic>\n            -induced Guillain-Barre\u0301 syndrome (GBS), molecular mimicry between\n            <jats:italic>C. jejuni<\/jats:italic>\n            lipooligosaccharide (LOS) and host gangliosides leads to the production of cross-reactive antibodies directed against the peripheral nerves of the host. Currently, the presence of surface exposed sialylated LOS in\n            <jats:italic>C. jejuni<\/jats:italic>\n            is the single known bacterial pathogenesis factor associated with the development of GBS. Using a unique, well-characterized strain collection, we demonstrate that GBS-associated\n            <jats:italic>C. jejuni<\/jats:italic>\n            strains bind preferentially to sialoadhesin (Sn, Siglec-1, or CD169), a sialic acid receptor found on a subset of macrophages. In addition, using a whole-cell enzyme-linked immunosorbent assay (ELISA),\n            <jats:italic>C. jejuni<\/jats:italic>\n            strains with sialylated LOS bound exclusively to soluble Sn. Mass spectrometry revealed that binding was sialic acid-linkage specific with a preference for \u03b1(2,3)-linked sialic acid attached to the terminal galactose of the LOS chain as seen in the gangliosides GD1a, GM1b, and GM3. This molecular interaction was also related to functional consequences as a GBS-associated\n            <jats:italic>C. jejuni<\/jats:italic>\n            strain that bound Sn in a whole-cell ELISA adhered to surface-expressed Sn of Sn-transfected CHO cells but was unable to adhere to wild-type CHO cells. Moreover, a sialic acid-negative mutant of the same\n            <jats:italic>C. jejuni<\/jats:italic>\n            strain was unable to bind Sn-transfected CHO cells. This is the first report of the preferential binding of GBS-associated\n            <jats:italic>C. jejuni<\/jats:italic>\n            strains to the Sn immune receptor (\n            <jats:italic>P<\/jats:italic>\n            = 0.014). Moreover, because this binding is dependent on sialylated LOS, the main pathogenic factor in GBS progression, the present findings bring us closer to unraveling the mechanisms that lead to formation of cross-reactive antibodies in GBS disease.\n          <\/jats:p>","DOI":"10.1128\/iai.01273-09","type":"journal-article","created":{"date-parts":[[2010,4,27]],"date-time":"2010-04-27T02:07:37Z","timestamp":1272334057000},"page":"3237-3246","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":89,"title":["Characterization of the Specific Interaction between Sialoadhesin and Sialylated\n            <i>Campylobacter jejuni<\/i>\n            Lipooligosaccharides"],"prefix":"10.1128","volume":"78","author":[{"given":"Astrid P.","family":"Heikema","sequence":"first","affiliation":[{"name":"Department of Medical Microbiology and Infectious Diseases"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mathijs P.","family":"Bergman","sequence":"additional","affiliation":[{"name":"Department of Molecular Microbiology, Faculty of Earth and Life Sciences, Vrije Universiteit Amsterdam, Amsterdam, Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hannah","family":"Richards","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul R.","family":"Crocker","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michel","family":"Gilbert","sequence":"additional","affiliation":[{"name":"Institute for Biological Sciences, Ottawa, Ontario, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janneke N.","family":"Samsom","sequence":"additional","affiliation":[{"name":"Laboratory of Pediatric Gastroenterology, Erasmus MC, University Medical Centre Rotterdam, Rotterdam, Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willem J. 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