ArticleInfection and immunity2008
Identification of TbpA residues required for transferrin-iron utilization by Neisseria gonorrhoeae.
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 23 papers.
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Who cites it
23 citing papers in PubMed.
- Rationally designed minimized TbpB confers broad protection against meningococcal infection.PLoS pathogens · 2026Article
- Structural insights into the mechanism underpinning iron piracy in pathogenicScience advances · 2026Article
- Investigating the importance of selected surface-exposed loops in HpuB for hemoglobin binding and utilization byInfection and immunity · 2024Article
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Bacterial Protein Tyrosine Phosphatases as Possible Targets for Antimicrobial Therapies in Response to Antibiotic Resistance.Antioxidants (Basel, Switzerland) · 2022Review
- Article
- Acclimation to Nutritional Immunity and Metal Intoxication Requires Zinc, Manganese, and Copper Homeostasis in the PathogenicFrontiers in cellular and infection microbiology · 2022Review
- Stealthy microbes: HowFrontiers in cellular and infection microbiology · 2022Review
- Structural Basis for Evasion of Nutritional Immunity by the PathogenicFrontiers in microbiology · 2019Review
- Quantitative Proteomics of the 2016 WHOMolecular & cellular proteomics : MCP · 2019Article
- Lipid-Modified Azurin ofFrontiers in microbiology · 2018Article
- Gonorrhea - an evolving disease of the new millennium.Microbial cell (Graz, Austria) · 2016Review
- Beyond the Crystal Structure: Insight into the Function and Vaccine Potential of TbpA Expressed by Neisseria gonorrhoeae.Infection and immunity · 2015Article
- Patterns of structural and sequence variation within isotype lineages of the Neisseria meningitidis transferrin receptor system.MicrobiologyOpen · 2015Article
- The transferrin-iron import system from pathogenic Neisseria species.Molecular microbiology · 2012Review
- Evidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transport.Metallomics : integrated biometal science · 2012Article
- Article
- Protection of mice from a Chlamydia trachomatis vaginal infection using a Salicylidene acylhydrazide, a potential microbicide.The Journal of infectious diseases · 2011Article
- TonB-Dependent Transporters Expressed by Neisseria gonorrhoeae.Frontiers in microbiology · 2011Article
- Candidate vaginal microbicides with activity against Chlamydia trachomatis and Neisseriagonorrhoeae.International journal of antimicrobial agents · 2010Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Neisseria gonorrhoeae requires iron for survival in the human host and therefore expresses high-affinity receptors for iron acquisition from host iron-binding proteins. The gonococcal transferrin-iron uptake system is composed of two transferrin binding proteins, TbpA and TbpB. TbpA is a TonB-dependent, outer membrane transporter critical for iron acquisition, while TbpB is a surface-exposed lipoprotein that increases the efficiency of iron uptake. The precise mechanism by which TbpA mediates iron acquisition has not been elucidated; however, the process is distinct from those of characterized siderophore transporters. Similar to these TonB-dependent transporters, TbpA is proposed to have two distinct domains, a beta-barrel and a plug domain. We hypothesize that the TbpA plug coordinates iron and therefore potentially functions in multiple steps of transferrin-mediated iron acquisition. To test this hypothesis, we targeted a conserved motif within the TbpA plug domain and generated single, double, and triple alanine substitution mutants. Mutagenized TbpAs were expressed on the gonococcal cell surface and maintained wild-type transferrin binding affinity. Single alanine substitution mutants internalized iron at wild-type levels, while the double and triple mutants showed a significant decrease in iron uptake. Moreover, the triple alanine substitution mutant was unable to grow on transferrin as a sole iron source; however, expression of TbpB compensated for this defect. These data indicate that the conserved motif between residues 120 and 122 of the TbpA plug domain is critical for transferrin-iron utilization, suggesting that this region plays a role in iron acquisition that is shared by both TbpA and TbpB.
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