ArticleVirulence2012
Study of streptococcal hemoprotein receptor (Shr) in iron acquisition and virulence of M1T1 group A streptococcus.
Article in Virulence, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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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
20 citing papers in PubMed, 38 citations in OpenAlex.
- The bacterial cell membrane acts as a dynamic heme reservoir during group BbioRxiv : the preprint server for biology · 2026Article
- Article
- Determinants of bacterial survival and proliferation in blood.FEMS microbiology reviews · 2024Review
- Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024Review
- Structural basis for the recognition of human hemoglobin by the heme-acquisition protein Shr from Streptococcus pyogenes.Scientific reports · 2024Article
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Native Human Antibody to Shr Promotes Mice Survival After Intraperitoneal Challenge With Invasive Group A Streptococcus.The Journal of infectious diseases · 2021Article
- Comparative Genomic Analysis ofFrontiers in microbiology · 2021Article
- A Novel Heme Transporter from the Energy Coupling Factor Family Is Vital for Group A Streptococcus Colonization and Infections.Journal of bacteriology · 2020Article
- Transcriptomic Analysis of Streptococcus pyogenes Colonizing the Vaginal Mucosa IdentifiesmBio · 2019Article
- TheThe Journal of biological chemistry · 2018Article
- The Heme Transporter HtsABC of Group AFrontiers in microbiology · 2018Article
- The Transcriptional Regulator CpsY Is Important for Innate Immune Evasion in Streptococcus pyogenes.Infection and immunity · 2017Article
- Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016Review
- Virulence factors of Streptococcus pyogenes strains from women in peri-labor with invasive infections.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016Article
- CovRS-Regulated Transcriptome Analysis of a Hypervirulent M23 Strain of Group A Streptococcus pyogenes Provides New Insights into Virulence Determinants.Journal of bacteriology · 2015Article
- Copper Tolerance and Characterization of a Copper-Responsive Operon, copYAZ, in an M1T1 Clinical Strain of Streptococcus pyogenes.Journal of bacteriology · 2015Article
- Mechanisms of group A Streptococcus resistance to reactive oxygen species.FEMS microbiology reviews · 2015Review
- Mutual exclusivity of hyaluronan and hyaluronidase in invasive group A Streptococcus.The Journal of biological chemistry · 2014Article
- The streptococcal hemoprotein receptor: a moonlighting protein or a virulence factor?Virulence · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Streptococcus pyogenes (group A streptococcus, GAS) is a human bacterial pathogen of global significance, causing severe invasive diseases associated with serious morbidity and mortality. To survive within the host and establish an infection, GAS requires essential nutrients, including iron. The streptococcal hemoprotein receptor (Shr) is a surface-localized GAS protein that binds heme-containing proteins and extracellular matrix components. In this study, we employ targeted allelic exchange mutagenesis to investigate the role of Shr in the pathogenesis of the globally disseminated serotype M1T1 GAS. The shr mutant exhibited a growth defect in iron-restricted medium supplemented with ferric chloride, but no significant differences were observed in neutrophil survival, antimicrobial peptide resistance, cell surface charge, fibronectin-binding or adherence to human epithelial cells and keratinocytes, compared with wild-type. However, the shr mutant displayed a reduction in human blood proliferation, laminin-binding capacity and was attenuated for virulence in in vivo models of skin and systemic infection. We conclude that Shr augments GAS adherence to laminin, an important extracellular matrix attachment component. Furthermore, Shr-mediated iron uptake contributes to GAS growth in human blood, and is required for full virulence of serotype M1T1 GAS in mouse models of invasive disease.
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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.