ArticleProceedings of the National Academy of Sciences of the United States of America2010
Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 76 citations in OpenAlex.
- Host glutathione is required for Rickettsia parkeri cell division and intracellular survival.Nature communications · 2025Article
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- Exploiting haem-iron dependence of nontypeableFrontiers in cellular and infection microbiology · 2025Review
- Molecular basis for substrate transport ofScience advances · 2024Article
- Antimicrobial Peptide Recognition Motif of the Substrate Binding Protein SapA from NontypeableBiochemistry · 2024Article
- Diverse roles of low-molecular weight thiol GSH inCurrent research in microbial sciences · 2024Article
- Discovery of a glutathione utilization pathway in Francisella that shows functional divergence between environmental and pathogenic species.Cell host & microbe · 2023Article
- Multiplatform Metabolomics Characterization Reveals Novel Metabolites and Phospholipid Compositional Rules ofInternational journal of molecular sciences · 2023Article
- Identification of a Novel Linear B-Cell Epitope of HbpA Protein fromInternational journal of molecular sciences · 2023Article
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- Genome-wide screening of lipoproteins in Actinobacillus pleuropneumoniae identifies three antigens that confer protection against virulent challenge.Scientific reports · 2020Article
- Moonlighting of Haemophilus influenzae heme acquisition systems contributes to the host airway-pathogen interplay in a coordinated manner.Virulence · 2019Article
- Molecular Basis of Unexpected Specificity of ABC Transporter-Associated Substrate-Binding Protein DppA from Helicobacter pylori.Journal of bacteriology · 2019Article
- Oligopeptide-binding protein from nontypeableThe Journal of biological chemistry · 2019Article
- Molecular characterization of the interaction of sialic acid with the periplasmic binding protein fromThe Journal of biological chemistry · 2018Article
- Purification and Characterization of Glutathione Binding Protein GsiB fromBioMed research international · 2018Article
- Structure and dynamics of Type III periplasmic proteins VcFhuD and VcHutB reveal molecular basis of their distinctive ligand binding properties.Scientific reports · 2017Article
- Evaluation of glutathione-binding protein A of Haemophilus parasuis as a vaccine candidate in a mouse model.The Journal of veterinary medical science · 2017Article
- Purification and Characterization of an ATPase GsiA fromBioMed research international · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione (GSH) is a vital intracellular cysteine-containing tripeptide across all kingdoms of life and assumes a plethora of cellular roles. Such pleiotropic behavior relies on a finely tuned spatiotemporal distribution of glutathione and its conjugates, which is not only controlled by synthesis and breakdown, but also by transport. Here, we show that import of glutathione in the obligate human pathogen Haemophilus influenzae, a glutathione auxotrophe, is mediated by the ATP-binding cassette (ABC)-like dipeptide transporter DppBCDF, which is primed for glutathione transport by a dedicated periplasmic-binding protein (PBP). We have identified the periplasmic lipoprotein HbpA, a protein hitherto implicated in heme acquisition, as the cognate PBP that specifically binds reduced (GSH) and oxidized glutathione (GSSG) forms of glutathione with physiologically relevant affinity, while it exhibits marginal binding to hemin. Dissection of the ligand preferences of HbpA showed that HbpA does not recognize bulky glutathione S conjugates or glutathione derivatives with C-terminal modifications, consistent with the need for selective import of useful forms of glutathione and the concomitant exclusion of potentially toxic glutathione adducts. Structural studies of the highly homologous HbpA from Haemophilus parasuis in complex with GSSG have revealed the structural basis of the proposed novel function for HbpA-like proteins, thus allowing a delineation of highly conserved structure-sequence fingerprints for the entire family of HbpA proteins. Taken together, our studies unmask the main physiological role of HbpA and establish a paradigm for glutathione import in bacteria. Accordingly, we propose a name change for HbpA to glutathione-binding protein A.
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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.