ArticleBMC microbiology2005
ABC transporter FtsABCD of Streptococcus pyogenes mediates uptake of ferric ferrichrome.
Article in BMC microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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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Who cites it
36 citing papers in PubMed, 62 citations in OpenAlex.
- Development of an inhibitory monoclonal nanobody targeting Streptococcus pyogenes siderophore binding protein FtsB.The Journal of biological chemistry · 2026Article
- Ferrichrome: bacterial function, synthetic mimics, and biomedical applications.Frontiers in microbiology · 2026Review
- Analysis ofmBio · 2025Article
- New insights into iron uptake in Streptococcus mutans: evidence for a role of siderophore-like molecules.Archives of microbiology · 2025Article
- Global spread of Streptococcus pyogenes A genomics-supported narrative review.FEMS microbiology reviews · 2025Review
- Bacterial siderophores: diversity, uptake pathways and applications.Nature reviews. Microbiology · 2025Review
- Metal Homeostasis in Pathogenic Streptococci.Microorganisms · 2022Review
- Immunization with the lipoprotein FtsB stimulates protective immunity againstFrontiers in microbiology · 2022Article
- A Novel Heme Transporter from the Energy Coupling Factor Family Is Vital for Group A Streptococcus Colonization and Infections.Journal of bacteriology · 2020Article
- Metal sensing and regulation of adaptive responses to manganese limitation by MtsR is critical for group A streptococcus virulence.Nucleic acids research · 2019Article
- Disruption of a Novel Iron Transport System Reverses Oxidative Stress Phenotypes of aJournal of bacteriology · 2018Article
- The Heme Transporter HtsABC of Group AFrontiers in microbiology · 2018Article
- The PerR-Regulated PInfection and immunity · 2017Article
- Inhibitory role of acyl homoserine lactones in hemolytic activity and viability of Streptococcus pyogenes M6 S165.Scientific reports · 2017Article
- Quantitative Proteomic Analysis Reveals Changes in the BenchmarkFrontiers in cellular and infection microbiology · 2017Article
- Mechanisms of group A Streptococcus resistance to reactive oxygen species.FEMS microbiology reviews · 2015Review
- A Neutralizing Monoclonal IgG1 Antibody of Platelet-Activating Factor Acetylhydrolase SsE Protects Mice against Lethal Subcutaneous Group A Streptococcus Infection.Infection and immunity · 2015Article
- Lipoprotein FtsB in Streptococcus pyogenes binds ferrichrome in two steps with residues Tyr137 and Trp204 as critical ligands.PloS one · 2013Article
- Review
- Extracellular heme uptake and the challenges of bacterial cell membranes.Current topics in membranes · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe Streptococcus pyogenes or Group A Streptococcus (GAS) genome encodes three ABC transporters, namely, FtsABCD, MtsABC, and HtsABC, which share homology with iron transporters. MtsABC and HtsABC are believed to take up ferric (Fe3+) and manganese ions and heme, respectively, while the specificity of FtsABCD is unknown.
resultsRecombinant FtsB, the lipoprotein component of FtsABCD, was found to bind Fe3+ ferrichrome in a 1:1 stoichiometry. To investigate whether FtsABCD transports Fe3+ ferrichrome, GAS isogenic strains defective in lipoprotein gene ftsB and permease gene ftsC were generated, and the effects of the mutations on uptake of Fe3+ ferrichrome were examined using radioactive 55Fe3+ ferrichrome. FtsB was produced in the wild-type strain but not in the ftsB mutant, confirming the ftsB inactivation. While wild-type GAS took up 3.6 x 10(4) Fe3+ ferrichrome molecules per bacterium per min at room temperature, the ftsB and ftsC mutants did not have a detectable rate of Fe3+ ferrichrome uptake. The inactivation of ftsB or ftsC also decreased 55Fe3+ ferrichrome uptake by >90% under growth conditions in the case of limited uptake time. Complementation of the ftsB mutant with a plasmid carrying the ftsB gene restored FtsB production and 55Fe3+ ferrichrome association at higher levels compared with the parent strain. The inactivation of mtsA and htsA and Fe-restricted conditions enhanced the production of FtsB and Fe3+ ferrichrome uptake.
conclusionThe FtsB protein bound Fe3+ ferrichrome, and inactivation of ftsB or ftsC, but not htsA or mtsA, diminished Fe3+ ferrichrome uptake, indicating that FtsABCD, but not HtsABC and MtsABC, is the transporter that takes up Fe3+ ferrichrome in GAS. Fe acquisition systems are virulence factors in many bacterial pathogens and are attractive vaccine candidates. The elucidation of the FtsABCD specificity advances the understanding of Fe acquisition processes in GAS and may help evaluating the GAS Fe acquisition systems as vaccine candidates.
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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.