The Novel Fibrinogen-Binding Protein FbsB Promotes<i>Streptococcus agalactiae</i>Invasion into Epithelial Cells

Gutekunst, Heike; Eikmanns, Bernhard J.; Reinscheid, Dieter J.

doi:10.1128/iai.72.6.3495-3504.2004

Cited by 92 publications

(102 citation statements)

References 83 publications

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“…The high upregulation of fbsB upon invasion of host cells is consistent with a previous study that showed that FbsB is important in invasion of epithelial cells but not in attachment (36). The ST-19 strain showed no expression of fbsB for any of the samples tested in this study.…”

Section: Discussionsupporting

confidence: 80%

Association and Virulence Gene Expression Vary among Serotype III Group B Streptococcus Isolates following Exposure to Decidual and Lung Epithelial Cells

et al. 2014

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Section: Discussionsupporting

confidence: 80%

Association and Virulence Gene Expression Vary among Serotype III Group B Streptococcus Isolates following Exposure to Decidual and Lung Epithelial Cells

et al. 2014

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“…The gene fbsB encodes a fibrinogen binding protein (37,38). Five hybridization patterns were generated by eight probes; isolates lacking fbsB were not observed.…”

Section: ) the Alleles Alp-2 Alp-3 Alp-4 (ϭ Alp-6) And Alp-5 (ϭ Amentioning

confidence: 99%

DNA Microarray-Based Typing of Streptococcus agalactiae Isolates

Nitschke¹,

Slickers²,

Müller³

et al. 2014

J Clin Microbiol

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c Streptococcus agalactiae frequently colonizes the urogenital tract, and it is a major cause of bacterial septicemia, meningitis, and pneumonia in newborns. For typing purposes, a microarray targeting group B streptococcus (GBS) virulence-associated markers and resistance genes was designed and validated with reference strains, as well as clinical and veterinary isolates. Selected isolates were also subjected to multilocus sequence typing. It was observed that putative typing markers, such as alleles of the alpha-like protein or capsule types, vary independently of each other, and they also vary independently from the affiliation to their multilocus sequence typing (MLST)-defined sequence types. Thus, it is not possible to assign isolates to sequence types based on the identification of a single distinct marker, such as a capsule type or alp allele. This suggests the occurrence of frequent genomic recombination. For array-based typing, a set of 11 markers (bac, alp, pil1 locus, pepS8, fbsB, capsule locus, hylB, abiG-I/-II plus Q8DZ34, pil2 locus, nss plus srr plus rogB2, and rgfC/A/D/B) was defined that provides a framework for splitting the tested 448 S. agalactiae isolates into 76 strains that clustered mainly according to MLST-defined clonal complexes. There was evidence for region-and host-specific differences in the population structure of S. agalactiae, as well as an overrepresentation of strains related to sequence type 17 among the invasive isolates. The arrays and typing scheme described here proved to be a convenient tool for genotyping large numbers of clinical/veterinary isolates and thus might help obtain insight into the epidemiology of S. agalactiae.

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“…Subsequent transmigration of S. agalactiae across the epithelial border allows the bacteria to invade the bloodstream and eventually reach the meninges [1]. Invasion of host cells represents an important mechanism in invasive S. agalactiae diseases [2,3].…”

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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The Novel Fibrinogen-Binding Protein FbsB PromotesStreptococcus agalactiaeInvasion into Epithelial Cells

Cited by 92 publications

References 83 publications

Association and Virulence Gene Expression Vary among Serotype III Group B Streptococcus Isolates following Exposure to Decidual and Lung Epithelial Cells

Association and Virulence Gene Expression Vary among Serotype III Group B Streptococcus Isolates following Exposure to Decidual and Lung Epithelial Cells

DNA Microarray-Based Typing of Streptococcus agalactiae Isolates

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

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