ArticlePLoS pathogens2010
beta-Neurexin is a ligand for the Staphylococcus aureus MSCRAMM SdrC.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed.
- The Neurexin1β Histidine-Rich Domain Is Involved in Excitatory Presynaptic Organization and Short-Term Plasticity.eNeuro · 2026Article
- Mechanism of antibacterial and antibiofilm of thiazolidinone derivative TD-H2-A against Staphylococcus aureus.Scientific reports · 2025Article
- Potential Therapeutic Targets for Combination Antibody Therapy AgainstAntibiotics (Basel, Switzerland) · 2024Review
- Adhesive Virulence Factors ofACS bio & med chem Au · 2022Article
- Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Identification of Three Clf-Sdr Subfamily Proteins inFrontiers in microbiology · 2021Article
- Article
- Staphylococcal Biofilm Development: Structure, Regulation, and Treatment Strategies.Microbiology and molecular biology reviews : MMBR · 2020Review
- "Gene accordions" cause genotypic and phenotypic heterogeneity in clonal populations of Staphylococcus aureus.Nature communications · 2020Article
- The Streptococcal Protease SpeB Antagonizes the Biofilms of the Human Pathogen Staphylococcus aureus USA300 through Cleavage of the Staphylococcal SdrC Protein.Journal of bacteriology · 2020Article
- Surface Proteins ofMicrobiology spectrum · 2019Review
- Sortases, Surface Proteins, and Their Roles inMicrobiology spectrum · 2019Article
- Genetic variability in the sdrD gene in Staphylococcus aureus from healthy nasal carriers.BMC microbiology · 2018Article
- Article
- Staphylococcal Biofilms in Atopic Dermatitis.Current allergy and asthma reports · 2017Review
- Molecular interactions and inhibition of the staphylococcal biofilm-forming protein SdrC.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Serine-Aspartate Repeat Protein D Increases Staphylococcus aureus Virulence and Survival in Blood.Infection and immunity · 2017Article
- Article
- Bacillus anthracis S-layer protein BslA binds to extracellular matrix by interacting with laminin.BMC microbiology · 2016Article
- The Staphylococcal Biofilm: Adhesins, Regulation, and Host Response.Microbiology spectrum · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Gram-positive bacteria contain a family of surface proteins that are covalently anchored to the cell wall of the organism. These cell-wall anchored (CWA) proteins appear to play key roles in the interactions between pathogenic organisms and the host. A subfamily of the CWA has a common structural organization with multiple domains adopting characteristic IgG-like folds. The identified microbial surface components recognizing adhesive matrix molecules (MSCRAMMs) belong to this subfamily, as does SdrC from S. aureus. However, an interactive host ligand for the putative MSCRAMM SdrC was not previously identified. We have screened a phage display peptide library and identified a peptide sequence found in beta-neurexin that binds SdrC. A synthetic peptide corresponding to the identified sequence as well as a recombinant form of the beta-neurexin 1 exodomain binds SdrC with high affinity and specificity. Furthermore, expression of SdrC on bacteria greatly enhances microbial adherence to cultured mammalian cells expressing beta-neurexin on their surface. Taken together, our experimental results demonstrate that beta-neurexin is a ligand for SdrC. This interaction involves a specific sequence located in the N-terminal region of the mammalian protein and the N(2)N(3) domain of the MSCRAMM. The fact that these two proteins interact when expressed on the appropriate cells demonstrates the functionality of the interaction. Possible implications of this interaction are discussed.
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.