ArticleThe Journal of biological chemistry2014
FbsC, a novel fibrinogen-binding protein, promotes Streptococcus agalactiae-host cell interactions.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 69 citations in OpenAlex.
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- Group B streptococcal infections in pregnancy and early life.Clinical microbiology reviews · 2025Review
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- Role of the SaeRS Two-Component Regulatory System in Group BMicroorganisms · 2024Article
- Re-framing the importance of Group BInfection and immunity · 2024Review
- Strain-level genomic analysis of serotype, genotype and virulence gene composition of group B streptococcus.Frontiers in cellular and infection microbiology · 2024Article
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- Group B Streptococcus: Virulence Factors and Pathogenic Mechanism.Microorganisms · 2022Review
- Nitric Oxide Production and Effects in Group BPathogens (Basel, Switzerland) · 2022Article
- Population genomics of Group B Streptococcus reveals the genetics of neonatal disease onset and meningeal invasion.Nature communications · 2022Article
- Streptococcus pneumoniae binds collagens and C1q via the SSURE repeats of the PfbB adhesin.Molecular microbiology · 2022Article
- Group B Streptococcal Neonatal Meningitis.Clinical microbiology reviews · 2022Review
- The pathogenesis of prevalent aerobic bacteria in aerobic vaginitis and adverse pregnancy outcomes: a narrative review.Reproductive health · 2022Review
- Protective role of IL-18 in host defenses against group B Streptococcus.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2021Article
- The CovR regulatory network drives the evolution of Group B Streptococcus virulence.PLoS genetics · 2021Article
- Article
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus agalactiae (group B Streptococcus or GBS) is a common cause of invasive infections in newborn infants and adults. The ability of GBS to bind human fibrinogen is of crucial importance in promoting colonization and invasion of host barriers. We characterized here a novel fibrinogen-binding protein of GBS, designated FbsC (Gbs0791), which is encoded by the prototype GBS strain NEM316. FbsC, which bears two bacterial immunoglobulin-like tandem repeat domains and a C-terminal cell wall-anchoring motif (LPXTG), was found to be covalently linked to the cell wall by the housekeeping sortase A. Studies using recombinant FbsC indicated that it binds fibrinogen in a dose-dependent and saturable manner, and with moderate affinity. Expression of FbsC was detected in all clinical GBS isolates, except those belonging to the hypervirulent lineage ST17. Deletion of fbsC decreases NEM316 abilities to adhere to and invade human epithelial and endothelial cells, and to form biofilm in vitro. Notably, bacterial adhesion to fibrinogen and fibrinogen binding to bacterial cells were abolished following fbsC deletion in NEM316. Moreover, the virulence of the fbsC deletion mutant and its ability to colonize the brain were impaired in murine models of infection. Finally, immunization with recombinant FbsC significantly protected mice from lethal GBS challenge. In conclusion, FbsC is a novel fibrinogen-binding protein expressed by most GBS isolates that functions as a virulence factor by promoting invasion of epithelial and endothelial barriers. In addition, the protein has significant immunoprotective activity and may be a useful component of an anti-GBS vaccine.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.