ArticleThe Journal of biological chemistry2013
Characterization of fibrinogen binding by glycoproteins Srr1 and Srr2 of Streptococcus agalactiae.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 110 citations in OpenAlex.
- Review
- Emergence, identification, and characterization of a novel Streptococcus agalactiae CPS type Ia ST7 strain (Ia-2021) causing large scale mortalities in tilapia aquaculture.Scientific reports · 2026Article
- Genomic epidemiology of Group B Streptococcus colonization among pregnant women in Japan, 2021-2023.PloS one · 2026Article
- Group B streptococcal infections in pregnancy and early life.Clinical microbiology reviews · 2025Review
- Analysis of serotype distribution and characteristics of nonhemolytic and nonpigmented strains among group B Streptococcus isolates in a southern Taiwan local hospital.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Re-framing the importance of Group BInfection and immunity · 2024Review
- The hypervirulent Group B Streptococcus HvgA adhesin promotes central nervous system invasion through transcellular crossing of the choroid plexus.Fluids and barriers of the CNS · 2024Article
- The serine-rich repeat glycoprotein Srr2 mediates Streptococcus agalactiae interaction with host fibronectin.BMC microbiology · 2024Article
- An opportunistic pathogen under stress: how Group B Streptococcus responds to cytotoxic reactive species and conditions of metal ion imbalance to survive.FEMS microbiology reviews · 2024Review
- Specific interaction between Group BInfection and immunity · 2024Article
- TGFβ1-induced hedgehog signaling suppresses the immune response of brain microvascular endothelial cells elicited by meningitic Escherichia coli.Cell communication and signaling : CCS · 2024Article
- Review
- Vaccines forFrontiers in immunology · 2024Review
- Strain-level genomic analysis of serotype, genotype and virulence gene composition of group B streptococcus.Frontiers in cellular and infection microbiology · 2024Article
- Genomic insights into the diversity, virulence, and antimicrobial resistance of group BFrontiers in cellular and infection microbiology · 2024Article
- Gamma-Irradiated Non-Capsule Group B Streptococcus Promotes T-Cell Dependent Immunity and Provides a Cross-Protective Reaction.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Molecular characteristics and antibiotic resistance mechanisms of clindamycin-resistantFrontiers in microbiology · 2023Article
- Coxsackievirus B3 infects and disrupts human induced-pluripotent stem cell derived brain-like endothelial cells.Frontiers in cellular and infection microbiology · 2023Article
- Group B Streptococcus: Virulence Factors and Pathogenic Mechanism.Microorganisms · 2022Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
The serine-rich repeat glycoproteins of Gram-positive bacteria comprise a large family of cell wall proteins. Streptococcus agalactiae (group B streptococcus, GBS) expresses either Srr1 or Srr2 on its surface, depending on the strain. Srr1 has recently been shown to bind fibrinogen, and this interaction contributes to the pathogenesis of GBS meningitis. Although strains expressing Srr2 appear to be hypervirulent, no ligand for this adhesin has been described. We now demonstrate that Srr2 also binds human fibrinogen and that this interaction promotes GBS attachment to endothelial cells. Recombinant Srr1 and Srr2 bound fibrinogen in vitro, with affinities of KD = 2.1 × 10(-5) and 3.7 × 10(-6) M, respectively, as measured by surface plasmon resonance spectroscopy. The binding site for Srr1 and Srr2 was localized to tandem repeats 6-8 of the fibrinogen Aα chain. The structures of both the Srr1 and Srr2 binding regions were determined and, in combination with mutagenesis studies, suggest that both Srr1 and Srr2 interact with a segment of these repeats via a "dock, lock, and latch" mechanism. Moreover, properties of the latch region may account for the increased affinity between Srr2 and fibrinogen. Together, these studies identify how greater affinity of Srr2 for fibrinogen may contribute to the increased virulence associated with Srr2-expressing strains.
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