ArticleProceedings of the National Academy of Sciences of the United States of America2005
Structure of the streptococcal cell wall C5a peptidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
31 citing papers in PubMed, 69 citations in OpenAlex.
- Dissecting the properties of circulating IgG against streptococcal pathogens through a combined systems antigenomics-serology workflow.Nature communications · 2025Article
- Serine protease RAYM_01812 (SspA) inhibits complement-mediated killing and monocyte chemotaxis and contributes to virulence ofVirulence · 2024Article
- Strain-level genomic analysis of serotype, genotype and virulence gene composition of group B streptococcus.Frontiers in cellular and infection microbiology · 2024Article
- Comparative Structure Analysis of the Multi-Domain, Cell Envelope Proteases of Lactic Acid Bacteria.Microorganisms · 2023Article
- Immunization with Multiple Virulence Factors Provides Maternal and Neonatal Protection against Group B Streptococcus Serotypes.Vaccines · 2023Article
- Auto- and Hetero-Catalytic Processing of the N-Terminal Propeptide Promotes the C-Terminal Fibronectin Type III Domain-Mediated Dimerization of a Thermostable Vpr-like Protease.Applied and environmental microbiology · 2022Article
- Review
- Article
- Novel Chimeric Multiepitope Vaccine for Streptococcosis Disease in Nile Tilapia (Oreochromis niloticus Linn.).Scientific reports · 2020Article
- Structure, dynamics and immunogenicity of a catalytically inactive CComputational and structural biotechnology journal · 2020Article
- Modeled Structure of the Cell Envelope Proteinase ofFrontiers in bioengineering and biotechnology · 2020Article
- Review
- The Pathogenic Factors from Oral Streptococci for Systemic Diseases.International journal of molecular sciences · 2019Review
- The Streptococcus agalactiae complement interfering protein combines multiple complement-inhibitory mechanisms by interacting with both C4 and C3 ligands.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Pathogenic adaptations of Colletotrichum fungi revealed by genome wide gene family evolutionary analyses.PloS one · 2018Article
- Review
- Progress toward a group B streptococcal vaccine.Human vaccines & immunotherapeutics · 2018Article
- Multi-functional mechanisms of immune evasion by the streptococcal complement inhibitor C5a peptidase.PLoS pathogens · 2017Article
- Characterization of a New S8 serine Protease from Marine SedimentaryFrontiers in microbiology · 2016Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The structure of a cell surface enzyme from a gram-positive pathogen has been determined to 2-A resolution. Gram-positive pathogens have a thick cell wall to which proteins and carbohydrate are covalently attached. Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. Structural analysis of a 949-residue fragment of the [D130A,S512A] mutant of SCP from group B Streptococcus (S. agalactiae, SCPB) revealed SCPB is composed of five distinct domains. The N-terminal subtilisin-like protease domain has a 134-residue protease-associated domain inserted into a loop between two beta-strands. This domain also contains one of two Arg-Gly-Asp (RGD) sequences found in SCPB. At the C terminus are three fibronectin type III (Fn) domains. The second RGD sequence is located between Fn1 and Fn2. Our analysis suggests that SCP binding to integrins by the RGD motifs may stabilize conformational changes required for substrate binding.
Indexed as
Identifiers
What OpenQuestion holds
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.