{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:52:00Z","timestamp":1786978320581,"version":"build-2736575974"},"reference-count":60,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2025,1,21]],"date-time":"2025-01-21T00:00:00Z","timestamp":1737417600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["2748\/7\u20101"],"award-info":[{"award-number":["2748\/7\u20101"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["2748\/8\u20101"],"award-info":[{"award-number":["2748\/8\u20101"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Macromolecular Bioscience"],"published-print":{"date-parts":[[2025,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Glycosaminoglycans (GAGs) play a pivotal role in pathogen attachment and entry into host cells, where the interaction with GAGs is critical for a diverse range of bacteria and viruses. This study focuses on elucidating the specific interactions between sulfated GAGs and the adhesin OmcB (Outer membrane complex protein B) of\n                    <jats:italic>Chlamydia<\/jats:italic>\n                    species, examining how structural characteristics of GAGs, such as sulfation degree and molecular weight, influence their binding affinity and thereby affect bacterial infectivity. A surface\u2010based binding assay is established to determine the binding constants of OmcB with various GAGs. It is shown that increased sulfation and higher molecular weight enhance GAG binding to OmcB. These findings are further validated using cell assays, which shows that the addition of sulfated GAGs reduces OmcB\u2010cell binding and inhibits the attachment of\n                    <jats:italic>C. pneumoniae<\/jats:italic>\n                    elementary bodies (EBs), underscoring the pivotal role of specific GAGs in chlamydial infections. Notably, heparin exhibites a stronger inhibitory effect on OmcB compare to GAGs with similar sulfation degrees and molecular weights, suggesting that particular molecular architectures may optimize binding interactions.\n                  <\/jats:p>","DOI":"10.1002\/mabi.202400443","type":"journal-article","created":{"date-parts":[[2025,1,22]],"date-time":"2025-01-22T01:04:16Z","timestamp":1737507856000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Sulfated Glycosaminoglycans as Inhibitors for Chlamydia Infections: Molecular Weight and Sulfation Dependence"],"prefix":"10.1002","volume":"25","author":[{"given":"Sebastian","family":"Wintgens","sequence":"first","affiliation":[{"name":"Heinrich\u2010 Heine\u2010 University D\u00fcsseldorf Faculty of Mathematics and Natural Sciences Institute for Functional Microbial Genomics  40204 D\u00fcsseldorf 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