{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T13:00:55Z","timestamp":1792155655919,"version":"4.4.0"},"reference-count":43,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"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":[[2015,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Endovascular infections caused by\n            <jats:named-content content-type=\"genus-species\">Staphylococcus aureus<\/jats:named-content>\n            involve interactions with fibronectin present as extracellular matrix or surface ligand on host cells. We examined the expression, structure, and binding activity of the two major\n            <jats:named-content content-type=\"genus-species\">S. aureus<\/jats:named-content>\n            fibronectin-binding proteins (FnBPA, FnBPB) in 10 distinct, methicillin-resistant clinical isolates from patients with either persistent or resolving bacteremia. The persistent bacteremia isolates (\n            <jats:italic>n<\/jats:italic>\n            = 5) formed significantly stronger bonds with immobilized fibronectin as determined by dynamic binding measurements performed with atomic force microscopy. Several notable differences were also observed when the results were grouped by clonal complex 5 (CC5) strains (\n            <jats:italic>n<\/jats:italic>\n            = 5) versus CC45 strains (\n            <jats:italic>n<\/jats:italic>\n            = 5). Fibronectin-binding receptors on CC5 formed stronger bonds with immobilized fibronectin (\n            <jats:italic>P<\/jats:italic>\n            &lt; 0.001). The\n            <jats:italic>fnbA<\/jats:italic>\n            gene was expressed at higher levels in CC45, whereas\n            <jats:italic>fnbB<\/jats:italic>\n            was found in only CC5 isolates. The\n            <jats:italic>fnbB<\/jats:italic>\n            gene was not sequenced because all CC45 isolates lacked this gene. Instead, comparisons were made for\n            <jats:italic>fnbA<\/jats:italic>\n            , which was present in all 10 isolates. Sequencing of\n            <jats:italic>fnbA<\/jats:italic>\n            revealed discrete differences within high-affinity, fibronectin-binding repeats (FnBRs) of FnBPA that included (i) 5-amino-acid polymorphisms in FnBR-9, FnBR-10, and FnBR-11 involving charged or polar side chains, (ii) an extra, 38-amino-acid repeat inserted between FnBR-9 and FnBR-10 exclusively seen in CC45 isolates, and (iii) CC5 isolates had the SVDFEED epitope in FnBR-11 (a sequence shown to be essential for fibronectin binding), while this sequence was replaced in all CC45 isolates with GIDFVED (a motif known to favor host cell invasion at the cost of reduced fibronectin binding). These complementary sequence and binding data suggest that differences in\n            <jats:italic>fnbA<\/jats:italic>\n            and\n            <jats:italic>fnbB<\/jats:italic>\n            , particularly polymorphisms and duplications in FnBPA, give\n            <jats:named-content content-type=\"genus-species\">S. aureus<\/jats:named-content>\n            two distinct advantages in human endovascular infections: (i) FnBPs similar to that of CC5 enhance ligand binding and foster initiation of disease, and (ii) CC45-like FnBPs promote cell invasion, a key attribute in persistent endovascular infections.\n          <\/jats:p>","DOI":"10.1128\/iai.01074-15","type":"journal-article","created":{"date-parts":[[2015,9,29]],"date-time":"2015-09-29T02:18:33Z","timestamp":1443493113000},"page":"4772-4780","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":28,"title":["Endovascular Infections Caused by Methicillin-Resistant Staphylococcus aureus Are Linked to Clonal Complex-Specific Alterations in Binding and Invasion Domains of Fibronectin-Binding Protein A as Well as the Occurrence of\n            <i>fnbB<\/i>"],"prefix":"10.1128","volume":"83","author":[{"given":"Yan Q.","family":"Xiong","sequence":"first","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"David Geffen School of Medicine at UCLA, Los Angeles, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Batu K.","family":"Sharma-Kuinkel","sequence":"additional","affiliation":[{"name":"Duke University Medical Center, Durham, North Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nadia N.","family":"Casillas-Ituarte","sequence":"additional","affiliation":[{"name":"Ohio State University, Columbus, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr.,","given":"Vance G.","family":"Fowler","sequence":"additional","affiliation":[{"name":"Duke University Medical Center, Durham, North Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Rude","sequence":"additional","affiliation":[{"name":"Duke University Medical Center, Durham, North Carolina, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alex C.","family":"DiBartola","sequence":"additional","affiliation":[{"name":"Ohio State University, Columbus, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberto D.","family":"Lins","sequence":"additional","affiliation":[{"name":"Oswaldo Cruz Foundation, Aggeu Magalh\u00e3es Research Center, Recife, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wessam","family":"Abdel-Hady","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, 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