{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T16:24:52Z","timestamp":1792599892986,"version":"4.5.0"},"reference-count":55,"publisher":"National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2003,6,10]]},"abstract":"<jats:p>\n                    Host cell binding is an essential step in colonization by many bacterial  pathogens, and the Lyme disease agent,\n                    <jats:italic>Borrelia burgdorferi<\/jats:italic>\n                    , which  colonizes multiple tissues, is capable of attachment to diverse cell types.  Glycosaminoglycans (GAGs) are ubiquitously expressed on mammalian cells and  are recognized by multiple\n                    <jats:italic>B. burgdorferi<\/jats:italic>\n                    surface proteins. We  previously showed that\n                    <jats:italic>B. burgdorferi<\/jats:italic>\n                    strains differ in the  particular spectrum of GAGs that they recognize, leading to differences in the  cultured mammalian cell types that they efficiently bind. The molecular basis  of these binding specificities remains undefined, due to the difficulty of  analyzing multiple, potentially redundant cell attachment pathways and to the  paucity of genetic tools for this pathogen. In the current study, we show that  the expression of decorin-binding protein (Dbp) A and\/or DbpB, two\n                    <jats:italic>B.  burgdorferi<\/jats:italic>\n                    surface proteins that bind GAGs, is sufficient to convert a  high-passage nonadherent\n                    <jats:italic>B. burgdorferi<\/jats:italic>\n                    strain into one that  efficiently binds 293 epithelial cells. Epithelial cell attachment was  mediated by dermatan sulfate, and, consistent with this GAG-binding  specificity, these recombinant strains did not bind EA-Hy926 endothelial  cells. The GAG-binding properties of bacteria expressing DbpB or DbpA were  distinguishable, and DbpB but not DbpA promoted spirochetal attachment to C6  glial cells. Thus, DbpA and DbpB may each play central but distinct roles in  cell type-specific binding by Lyme disease spirochetes. This study illustrates  that transformation of high-passage\n                    <jats:italic>B. burgdorferi<\/jats:italic>\n                    strains may  provide a relatively simple genetic approach to analyze virulence-associated  phenotypes conferred by multiple bacterial factors.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1231043100","type":"journal-article","created":{"date-parts":[[2003,6,10]],"date-time":"2003-06-10T13:06:36Z","timestamp":1055250396000},"page":"7307-7312","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":105,"title":["Decorin-binding proteins A and B confer distinct mammalian cell  type-specific attachment by\n                    <i>Borrelia burgdorferi<\/i>\n                    , the Lyme disease  spirochete"],"prefix":"10.1073","volume":"100","author":[{"given":"Joshua R.","family":"Fischer","sequence":"first","affiliation":[{"name":"Department of Molecular Genetics and Microbiology, University 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