ArticleInfection and immunity2006
High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- A CRISPRi library screen in group BInfection and immunity · 2025Article
- A CRISPRi Library Screen in Group BbioRxiv : the preprint server for biology · 2024Article
- A 3D Bioprinted Gut Anaerobic Model for Studying Bacteria-Host Interactions.Research (Washington, D.C.) · 2023Article
- Mast cell-derived factor XIIIA contributes to sexual dimorphic defense against group B streptococcal infections.The Journal of clinical investigation · 2022Article
- The Role of Streptococcal Cell-Envelope Proteases in Bacterial Evasion of the Innate Immune System.Journal of innate immunity · 2022Review
- Potential factors involved in the early pathogenesis of Streptococcus uberis mastitis: a review.Folia microbiologica · 2021Review
- Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Review
- The Pathogenic Factors from Oral Streptococci for Systemic Diseases.International journal of molecular sciences · 2019Review
- The Double Life of Group B Streptococcus: Asymptomatic Colonizer and Potent Pathogen.Journal of molecular biology · 2019Review
- Review
- Vascular binding of a pathogen under shear force through mechanistically distinct sequential interactions with host macromolecules.Molecular microbiology · 2012Article
- Kinetics of leucine-lysine peptide adsorption and desorption at -CH3 and -COOH terminated alkylthiolate monolayers.Biointerphases · 2010Article
- Article
- Adhesion determinants of the Streptococcus species.Microbial biotechnology · 2010Review
- Human serum induces streptococcal c5a peptidase expression.Infection and immunity · 2009Article
- Streptococcus adherence and colonization.Microbiology and molecular biology reviews : MMBR · 2009Review
- Understanding the regulation of Group B Streptococcal virulence factors.Future microbiology · 2009Review
- Recent advances in understanding the molecular basis of group B Streptococcus virulence.Expert reviews in molecular medicine · 2008Review
- Interactions of the streptococcal C5a peptidase with human fibronectin.Acta biomaterialia · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The streptococcal C5a peptidase (ScpB) of group B streptococci (GBS) is found in virtually all clinical GBS isolates and is required for mucosal colonization in a neonatal mouse model. ScpB inhibits neutrophil chemotaxis by enzymatically cleaving the complement component C5a. We previously identified a second function of ScpB as a fibronectin (Fn) adhesin using phage display. However, phage display can identify low-affinity interactions. We therefore measured the affinity of both full-length recombinant ScpB (FL-ScpB) and the 110-amino-acid phage display fragment (Scp-PDF) for immobilized Fn using surface plasmon resonance. The affinity for Fn was very high for both FL-ScpB (equilibrium dissociation constant [KD] = 4.0 nM) and Scp-PDF (KD = 4.4 nM) and is consistent with a biologically significant role for the adhesin activity of ScpB. We also studied the Fn adhesin activity of a common natural variant of ScpB (ScpBDelta) that contains a 4-amino-acid deletion that eliminates peptidase activity. The integrity of scpB is otherwise maintained, suggesting that the Fn adhesin activity of ScpB may be responsible for its conservation in these strains. The affinities of both FL-ScpBDelta (KD = 2.4 nM) and ScpBDelta-PDF (KD = 1.4 nM) for Fn are unaffected by the deletion. Complementation in trans by both scpB and scpBDelta corrected the Fn-binding defect of an scpB deletion mutant GBS strain to an identical degree. The high affinity of ScpB for Fn and the maintenance of this affinity in ScpBDelta support our hypothesis that the Fn adhesin activity of scpB plays a role in virulence.
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Registered trials
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.