Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Point Mutations in TbpA Abrogate Human Transferrin Binding in Neisseria gonorrhoeae

2 Nov 2022

Abstract excerpt

TonB-dependent transporters (TDTs) are essential proteins for metal acquisition, an important step in the growth and pathogenesis of many pathogens, including Neisseria gonorrhoeae , the causative agent of gonorrhea. There is currently no available vaccine for gonorrhea; TDTs are being investigated as vaccine candidates because they are highly conserved and expressed in vivo .

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amoebic Infections and Treatments
Share to Bacterial Infections and Vaccines
Share to Reproductive tract infections research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36321833
DOI: 10.1128/iai.00414-22

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Point Mutations in TbpA Abrogate Human Transferrin Binding in Neisseria gonorrhoeaePMID 36321833Read ↗

TonB-Dependent Transporters Expressed by Neisseria gonorrhoeaeSemantic proximity Read ↗

Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptorsSemantic proximity Read ↗

Investigating the importance of selected surface-exposed loops in HpuB for hemoglobin binding and utilization by Neisseria gonorrhoeae.Semantic proximity Read ↗

The transferrin–iron import system from pathogenic N eisseria speciesSemantic proximity Read ↗

Investigating the importance of surface exposed loops in the gonococcal HpuB transporter for hemoglobin binding and utilizationSemantic proximity Read ↗

Structure-based engineering of a nutrient acquisition protein enhances neutralizing antibodies and protection for the development of a gonococcal vaccineSemantic proximity Read ↗

Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions.Semantic proximity Read ↗

Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilizationSemantic proximity Read ↗

Structural Basis for Evasion of Nutritional Immunity by the Pathogenic NeisseriaeSemantic proximity Read ↗

Rational selection of TbpB variants elucidates a bivalent vaccine formulation with broad spectrum coverage against <i>Neisseria gonorrhoeae</i>Semantic proximity Read ↗

Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins.Semantic proximity Read ↗

Mechanisms of iron acquisition by the human pathogens Neisseria Meningitidis and Neisseria GonorrhoeaeSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.