ReviewMolecular oral microbiology2012
A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis.
Review in Molecular oral microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 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
62 citing papers in PubMed.
- Oral streptococci utilize a Siglec-like domain of serine-rich repeat adhesins to preferentially target platelet sialoglycans in human blood.PLoS pathogens · 2014Trial
- Genetic engineering ofMicrobial genomics · 2026Article
- 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
- Exploiting strong synergies between punicalagin and cefoperazone to combat methicillin-resistant Staphylococcus aureus infections.NPJ biofilms and microbiomes · 2025Article
- Article
- Low-complexity regions in fungi display functional groups and are depleted in positively charged amino acids.NAR genomics and bioinformatics · 2025Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- The role of the glycome in symbiotic host-microbe interactions.Glycobiology · 2023Review
- Prevalence and Homology of the Pneumococcal Serine-Rich Repeat Protein at the Global Scale.Microbiology spectrum · 2023Article
- Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.Nature communications · 2022Article
- Pneumococcal Surface Proteins as Virulence Factors, Immunogens, and Conserved Vaccine Targets.Frontiers in cellular and infection microbiology · 2022Review
- Glycosyltransferases within theJournal of bacteriology · 2021Article
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- Opportunities and Challenges of Bacterial Glycosylation for the Development of Novel Antibacterial Strategies.Frontiers in microbiology · 2021Review
- Identification of Three Clf-Sdr Subfamily Proteins inFrontiers in microbiology · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Review
- Structure based virtual screening identifies small molecule effectors for the sialoglycan binding protein Hsa.The Biochemical journal · 2020Article
- Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.Biomolecular NMR assignments · 2020Article
- Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity.Microorganisms · 2020Review
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Bacterial attachment to host surfaces is a pivotal event in the biological and infectious processes of both commensal and pathogenic bacteria, respectively. Serine-rich repeat proteins (SRRPs) are a family of adhesins in Gram-positive bacteria that mediate attachment to a variety of host and bacterial surfaces. As such, they contribute towards a wide-range of diseases including sub-acute bacterial endocarditis, community-acquired pneumonia, and meningitis. SRRPs are unique in that they are glycosylated, require a non-canonical Sec-translocase for transport, and are largely composed of a domain containing hundreds of alternating serine residues. These serine-rich repeats are thought to extend a unique non-repeat (NR) domain outward away from the bacterial surface to mediate adhesion. So far, NR domains have been determined to bind to sialic acid moieties, keratins, or other NR domains of a similar SRRP. This review summarizes how this important family of bacterial adhesins mediates bacterial attachment to host and bacterial cells, contributes to disease pathogenesis, and might be targeted for pharmacological intervention or used as novel protective vaccine antigens. This review also highlights recent structural findings on the NR domains of these proteins.
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.