{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T02:00:08Z","timestamp":1790128808842,"version":"4.0.1"},"reference-count":46,"publisher":"Microbiology Society","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,8,1]]},"abstract":"<jats:p><jats:italic>Bacteroides fragilis<\/jats:italic>is a bacterium that resides in the normal human gastro-intestinal tract; however, it is also the most commonly isolated Gram-negative obligate anaerobe from human clinical infections, such as intra-abdominal abscesses, and the most common cause of anaerobic bacteraemia. Abscess formation is important in bacterial containment, limiting dissemination of infection and bacteraemia. In this study, we investigated<jats:italic>B. fragilis<\/jats:italic>binding and degradation of human fibrinogen, the major structural component involved in fibrin abscess formation. We have shown that<jats:italic>B. fragilis<\/jats:italic>NCTC9343 binds human fibrinogen. A putative<jats:italic>Bacteroides<\/jats:italic><jats:italic>fragilis<\/jats:italic>fibrinogen-binding protein, designated BF-FBP, identified in the genome sequence of NCTC9343, was cloned and expressed in<jats:italic>Escherichia coli<\/jats:italic>. The purified recombinant BF-FBP bound primarily to the human fibrinogen B<jats:italic>\u03b2<\/jats:italic>-chain. In addition, we have identified fibrinogenolytic activity in<jats:italic>B. fragilis<\/jats:italic>exponential phase culture supernatants, associated with fibrinogenolytic metalloproteases in NCTC9343 and 638R, and cysteine protease activity in YCH46. All nine clinical isolates of<jats:italic>B. fragilis<\/jats:italic>examined degraded human fibrinogen; with eight isolates, initial A<jats:italic>\u03b1<\/jats:italic>-chain degradation was observed, with varying B<jats:italic>\u03b2<\/jats:italic>-chain and<jats:italic>\u03b3<\/jats:italic>-chain degradation. With one blood culture isolate, B<jats:italic>\u03b2<\/jats:italic>-chain and<jats:italic>\u03b3<\/jats:italic>-chain degradation occurred first, followed by subsequent A<jats:italic>\u03b1<\/jats:italic>-chain degradation. Our data raise the possibility that the fibrinogen-binding protein of<jats:italic>B. fragilis<\/jats:italic>, along with a variety of fibrinogenolytic proteases, may be an important virulence factor that facilitates dissemination of infection via reduction or inhibition of abscess formation.<\/jats:p>","DOI":"10.1099\/mic.0.038588-0","type":"journal-article","created":{"date-parts":[[2010,5,14]],"date-time":"2010-05-14T00:35:53Z","timestamp":1273797353000},"page":"2516-2526","source":"Crossref","is-referenced-by-count":26,"title":["Binding and degradation of fibrinogen by Bacteroides fragilis and characterization of a 54\u2005kDa fibrinogen-binding protein"],"prefix":"10.1099","volume":"156","author":[{"given":"Simon","family":"Houston","sequence":"first","affiliation":[{"name":"Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, 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