ArticleInfection and immunity2002
The group B streptococcal C5a peptidase is both a specific protease and an invasin.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 83 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
83 citing papers in PubMed, 166 citations in OpenAlex.
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- Virulence and pathogenicity of group BVirulence · 2025Review
- Identification of glyoxalase A in group BInfection and immunity · 2025Article
- A CRISPRi library screen in group BInfection and immunity · 2025Article
- Group B streptococcal infections in pregnancy and early life.Clinical microbiology reviews · 2025Review
- Molecular characterization of Streptococcus agalactiae strains isolated from pregnant women.Scientific reports · 2025Article
- 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
- Global spread of Streptococcus pyogenes A genomics-supported narrative review.FEMS microbiology reviews · 2025Review
- Identification of Glyoxalase A in Group BbioRxiv : the preprint server for biology · 2024Article
- A CRISPRi Library Screen in Group BbioRxiv : the preprint server for biology · 2024Article
- Serine protease RAYM_01812 (SspA) inhibits complement-mediated killing and monocyte chemotaxis and contributes to virulence ofVirulence · 2024Article
- Re-framing the importance of Group BInfection and immunity · 2024Review
- Genomic and functional determinants of host spectrum in Group B Streptococcus.PLoS pathogens · 2024Article
- Ecological, beneficial, and pathogenic functions of the Type 9 Secretion System.Microbial biotechnology · 2024Review
- 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
- Article
- Microbial evasion of the complement system: a continuous and evolving story.Frontiers in immunology · 2023Review
- The structure ofFrontiers in immunology · 2023Article
- A Novel Conserved Protein in Streptococcus agalactiae, BvaP, Is Important for Vaginal Colonization and Biofilm Formation.mSphere · 2022Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The group B streptococcus (GBS) is a major cause of pneumonia, sepsis, and meningitis in neonates and a serious cause of mortality or morbidity in immunocompromised adults. Although these streptococci adhere efficiently and invade a variety of tissue-specific epithelial and endothelial cells, adhesins and invasins are still unknown. All serotypes of GBS studied to date express C5a peptidase (SCPB) on their surface. This investigation addresses the possibility that this relatively large surface protein has additional activities. Rabbit anti-SCPB serum inhibited invasion of lung epithelial A549 cells by the serotype Ia strain O90R, suggesting that SCPB is an invasin. This was confirmed by inserting an in-frame 25-amino-acid deletion into the scpB gene. Invasion of HEp2 and A549 human cell lines was significantly reduced by the mutation. Enzyme-linked immunosorbent assays were used to demonstrate that purified SCPB protein binds directly to HEp2 and A549 cells and also binds the extracellular matrix protein fibronectin. Binding was dose dependent and saturable. These results suggested that SCPB is one of several potential invasins essential for GBS colonization of damaged epithelium.
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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.