ArticleInfection and immunity2008
Shr is a broad-spectrum surface receptor that contributes to adherence and virulence in group A streptococcus.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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.
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Who cites it
42 citing papers in PubMed, 88 citations in OpenAlex.
- Rational selection of antigenic targets for Group A Streptococcus vaccine: updates, challenges and opportunities.NPJ vaccines · 2026Review
- Rhamnose polysaccharide-decorated outer membrane vesicles as a vaccine candidate targeting Group A Streptococcus fromVaccine: X · 2025Article
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- Native Human Antibody to Shr Promotes Mice Survival After Intraperitoneal Challenge With Invasive Group A Streptococcus.The Journal of infectious diseases · 2021Article
- A Novel Heme Transporter from the Energy Coupling Factor Family Is Vital for Group A Streptococcus Colonization and Infections.Journal of bacteriology · 2020Article
- Review
- Transcriptomic Analysis of Streptococcus pyogenes Colonizing the Vaginal Mucosa IdentifiesmBio · 2019Article
- Extracellular Matrix Interactions with Gram-Positive Pathogens.Microbiology spectrum · 2019Review
- TheThe Journal of biological chemistry · 2018Article
- The Streptococcus pyogenes fibronectin/tenascin-binding protein PrtF.2 contributes to virulence in an influenza superinfection.Scientific reports · 2018Article
- Corynebacterium diphtheriae Iron-Regulated Surface Protein HbpA Is Involved in the Utilization of the Hemoglobin-Haptoglobin Complex as an Iron Source.Journal of bacteriology · 2018Article
- Article
- The Heme Transporter HtsABC of Group AFrontiers in microbiology · 2018Article
- Towards developing a vaccine for rheumatic heart disease.Global cardiology science & practice · 2017Review
- Collagen-like proteins of pathogenic streptococci.Molecular microbiology · 2017Review
- Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.Journal of inorganic biochemistry · 2016Article
- Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.PloS one · 2016Article
- Stuck in the Middle: Fibronectin-Binding Proteins in Gram-Positive Bacteria.Frontiers in microbiology · 2016Review
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Group A streptococcus (GAS) is a common hemolytic pathogen that produces a range of suppurative infections and autoimmune sequelae in humans. Shr is an exported protein in GAS, which binds in vitro to hemoglobin, myoglobin, and the hemoglobin-haptoglobin complex. We previously reported that Shr is found in association with whole GAS cells and in culture supernatant. Here, we demonstrate that cell-associated Shr could not be released from the bacteria by the muralytic enzyme mutanolysin and was instead localized to the membrane. Shr was available, however, on the exterior of GAS, exposed to the extracellular environment. In vitro binding and competition assays demonstrated that in addition to hemoprotein binding, purified Shr specifically interacts with immobilized fibronectin and laminin. The absence of typical fibronectin-binding motifs indicates that a new protein pattern is involved in the binding of Shr to the extracellular matrix. Recombinant Lactococcus lactis cells expressing Shr on the bacterial surface gained the ability to bind to immobilized fibronectin, suggesting that Shr can function as an adhesin. The inactivation of shr resulted in a 40% reduction in the attachment to human epithelial cells in comparison to the parent strain. GAS infection elicited a high titer of Shr antibodies in sera from convalescent mice, demonstrating that Shr is expressed in vivo. The shr mutant was attenuated for virulence in an intramuscular zebrafish model system. In summary, this study identifies Shr as being a new microbial surface component recognizing adhesive matrix molecules in GAS that mediates attachment to epithelial cells and contributes to the infection process.
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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.