ArticleNature communications2015
Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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
19 citing papers in PubMed.
- Porphyrin pathways as targets for combating antimicrobial resistance: virulence and therapeutic opportunities.Frontiers in cellular and infection microbiology · 2026Review
- Molecular basis of hemoglobin binding and heme removal inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Shr receptor fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022Review
- A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii.Nature communications · 2021Article
- An Exposed Outer Membrane Hemin-Binding Protein Facilitates Hemin Transport by a TonB-Dependent Receptor in Riemerella anatipestifer.Applied and environmental microbiology · 2021Article
- Intrauterine Growth Restriction Is Associated with Unique Features of the Reproductive Microbiome.Reproductive sciences (Thousand Oaks, Calif.) · 2021Article
- Metal-Limited Growth of Neisseria gonorrhoeae for Characterization of Metal-Responsive Genes and Metal Acquisition from Host Ligands.Journal of visualized experiments : JoVE · 2020Article
- Structural Basis for Evasion of Nutritional Immunity by the PathogenicFrontiers in microbiology · 2019Review
- TheThe Journal of biological chemistry · 2018Article
- The response of ruminal fermentation, epithelium-associated microbiota, and epithelial barrier function to severe feed restriction in pregnant ewes.Journal of animal science · 2018Article
- The Diversity of Mammalian Hemoproteins and Microbial Heme Scavengers Is Shaped by an Arms Race for Iron Piracy.Frontiers in immunology · 2018Article
- The Bacteriology and Its Virulence Factors in Neonatal Infections: Threats to Child Survival Strategies.Journal of pathogens · 2018Article
- Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017Review
- Identification of a Large Family of Slam-Dependent Surface Lipoproteins in Gram-Negative Bacteria.Frontiers in cellular and infection microbiology · 2017Article
- The Salmonella Effector SpvD Is a Cysteine Hydrolase with a Serovar-specific Polymorphism Influencing Catalytic Activity, Suppression of Immune Responses, and Bacterial Virulence.The Journal of biological chemistry · 2016Article
- Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016Review
- The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The Neisseriaceae family of bacteria causes a range of diseases including meningitis, septicaemia, gonorrhoea and endocarditis, and extracts haem from haemoglobin as an important iron source within the iron-limited environment of its human host. Herein we report crystal structures of apo- and haemoglobin-bound HpuA, an essential component of this haem import system. The interface involves long loops on the bacterial receptor that present hydrophobic side chains for packing against the surface of haemoglobin. Interestingly, our structural and biochemical analyses of Kingella denitrificans and Neisseria gonorrhoeae HpuA mutants, although validating the interactions observed in the crystal structure, show how Neisseriaceae have the fascinating ability to diversify functional sequences and yet retain the haemoglobin binding function. Our results present the first description of HpuA's role in direct binding of haemoglobin.
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