A fibrinogen receptor from group B <i>Streptococcus</i> interacts with fibrinogen by repetitive units with novel ligand binding sites

Schubert, Axel; Zakikhany, Katherina; Schreiner, Mark E.; Frank, Ronald; Spellerberg, Barbara; Eikmanns, Bernhard J.; Reinscheid, Dieter J.

doi:10.1046/j.1365-2958.2002.03177.x

Cited by 106 publications

(147 citation statements)

References 50 publications

(70 reference statements)

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“…In contrast to S. aureus (Dickinson et al 1995, MacFaddin 2000, S. epidermidis strains have the ability to adhere weakly to Fbn and express clumping activity, but they do not express free coagulase activity, detected by the tube procedure, which would lead to fibrin clotting (Christensen et al 1983, Nilsson et al 1998). The present data show that C. diphtheriae strains may bind Fbn onto their surface, which may be an efficient trait to avoid phagocytosis, as previously described with other Gram-positive pathogens (Schubert et al 2002, Rennermalm et al 2004, Pierno et al 2006. Bacterial aggregation by nontoxigenic ATCC 27010 was observed only in the presence of crude chelated plasma, whereas the other strains also expressed bacterial aggregates with diluted plasma, suggesting qualitative and/or quantitative differences in the expression of clumping activity by C. diphtheriae.…”

Section: Discussionsupporting

confidence: 82%

Fibrinogen binds to nontoxigenic and toxigenic Corynebacterium diphtheriae strains

Sabbadini

Genovez

Silva

et al. 2010

Mem. Inst. Oswaldo Cruz

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Section: Discussionsupporting

confidence: 82%

Fibrinogen binds to nontoxigenic and toxigenic Corynebacterium diphtheriae strains

Sabbadini

Genovez

Silva

et al. 2010

Mem. Inst. Oswaldo Cruz

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“…This bacterium also expresses a Fg receptor named FbsA that binds to human Fg [18]. Therefore, GBS cells have the potential to bind Plg through the direct and indirect pathways.…”

Section: Introductionmentioning

confidence: 99%

Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model

Magalhães

Veiga-Malta²,

Almeida³

et al. 2007

Microbes and Infection

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Interactions of several microbial pathogens with the plasminogen system increase their invasive potential. In this study, we show that Streptococcus agalactiae binds human plasminogen which can be subsequently activated to plasmin, thus generating a proteolytic bacterium. S. agalactiae binds plasminogen via the direct pathway, using plasminogen receptors, and via the indirect pathway through fibrinogen receptors. The glyceraldehyde-3-phosphate dehydrogenase is one of the S. agalactiae proteins that bind plasminogen. Presence of exogenous activators such as uPA and tPA are required to activate bound plasminogen. Results from competitive inhibition assays indicate that binding is partially mediated through the lysine binding sites of plasminogen. Following plasminogen binding and activation, S. agalactiae is able to degrade in vitro fibronectin, one of the host extracellular matrix proteins. Moreover, incubation of S. agalactiae with either plasminogen alone, or plasminogen plus fibrinogen, in the presence of tPA enhanced its virulence in C57BL/6 mice, suggesting that acquisition of plasmin-like activity by the bacteria increase their invasiveness.

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“…GBS adhesion is required for colonization and subsequent invasion. Several GBS surface proteins bind host extracellular matrix components and serum proteins (Beckmann et al, 2002;Gutekunst et al, 2004;Schubert et al, 2002;Spellerberg et al, 1999). ACP, a virulence factor and prototype for the Alp family of proteins, is the first surface protein identified to bind integral host cell-surface receptors, GAGs and a 1 b 1 -integrin.…”

Section: Discussionmentioning

confidence: 99%

The group B streptococcal alpha C protein binds α 1 β 1-integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells

Bolduc

Madoff

2007

Microbiology

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Group B Streptococcus (GBS) is the leading cause of bacterial pneumonia, sepsis and meningitis among neonates and a cause of morbidity among pregnant women and immunocompromised adults. GBS epithelial cell invasion is associated with expression of alpha C protein (ACP). Loss of ACP expression results in a decrease in GBS internalization and translocation across human cervical epithelial cells (ME180). Soluble ACP and its 170 amino acid N-terminal region (NtACP), but not the repeat protein RR9, bind to ME180 cells and reduce internalization of wild-type GBS to levels obtained with an ACP-deficient isogenic mutant. In the current study, ACP colocalized with a 1 b 1 -integrin, resulting in integrin clustering as determined by laser scanning confocal microscopy. NtACP contains two structural domains, D1 and D2. D1 is structurally similar to fibronectin's integrin-binding region (FnIII10). D1's (KT)D146 motif is structurally similar to the FnIII10 (RG)D1495 integrin-binding motif, suggesting that ACP binds a 1 b 1 -integrin via the D1 domain. The (KT)D146A mutation within soluble NtACP reduced its ability to bind a 1 b 1 -integrin and inhibit GBS internalization within ME180 cells. Thus ACP binding to human epithelial cell integrins appears to contribute to GBS internalization within epithelial cells. INTRODUCTIONGroup B Streptococcus (GBS; Streptococcus agalactiae) is the leading cause of neonatal bacterial invasive diseases (Arisoy et al., 2003;Manning et al., 2004). The organism colonizes the vagina, rectum and urethra of 10-35 % of adults without causing disease. Neonates acquire GBS either in utero or during birth, aspirating GBS-containing fluid. GBS enters the lungs, binds to and invades the alveolar epithelial cells, and enters the blood, allowing the organisms to infect multiple organs. Invasive disease occurs within hours of birth, with 4-6 % mortality (Baker & Edwards, 1995;Schrag et al., 2000). In a survey in the USA, the incidence of early-onset disease (within the first week of life) declined by 65 % (from 1.7 per 1000 live births to 0.6 per 1000) from 1993 to 1998, due to intrapartum antimicrobial prophylaxis (Schrag et al., 2000) and stabilized at 0.35 per 1000 in 2004 . The incidence of late-onset disease (.1 week to 3 months of age) remained stable, with an average of 0.35 per 1000 live births during the same time period (CDC, 1997(CDC, , 2005.GBS was more recently found to be pathogenic in the elderly, and in adults with underlying medical conditions, including diabetes (Dahl et al., 2003;Jackson et al., 1995;Tyrrell et al., 2000). Adult invasive GBS diseases result in bacteraemia, meningitis, skin and soft-tissue infection, and bone and joint infections. The rate of invasive diseases is significantly higher in neonates than in adults. However, the case fatality rates are greater in adults (Schuchat, 1999), with the incidence of GBS disease increasing with advanced age (Farley et al., 1993). Despite the clinical importance of these diseases, little is known about the events that lead up to GBS inv...

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A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites

Abstract: Summary Group B Streptococcus (GBS) is a frequent cause of bacterial sepsis and meningitis in neonates. During the course of infection, GBS colonizes and invades

Cited by 106 publications

References 50 publications

Fibrinogen binds to nontoxigenic and toxigenic Corynebacterium diphtheriae strains

Fibrinogen binds to nontoxigenic and toxigenic Corynebacterium diphtheriae strains

Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model

The group B streptococcal alpha C protein binds α 1 β 1-integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells

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