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

Acquisition of heme iron by Neisseria meningitidis does not involve meningococcal transferrin-binding proteins.

Infection and immunity - 1 Feb 1994

Martel N, Lee B C

Abstract excerpt

Similarities in size between hemin-binding protein 1 (HmBP1) and transferrin-binding protein 1 (TBP1) of Neisseria meningitidis suggest that these proteins are functionally homologous. However, a meningococcal mutant lacking the transferrin-binding proteins retained the capacity to acquire iron from heme and hemoglobin. In immunoblots, hyperimmune polyclonal antiserum against TBP1 did not react with HmBP1.

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Bacterial
Share to Carrier Proteins
Share to Cattle

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hemoglobins

Share to In Vitro Techniques

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 8300227
DOI: 10.1128/iai.62.2.700-703.1994
PMCID: PMC186161

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Acquisition of heme iron by Neisseria meningitidis does not involve meningococcal transferrin-binding proteins.PMID 8300227Read ↗

Iron Transport Systems in <i>Neisseria meningitidis</i>Semantic proximity Read ↗

Investigation into the Antigenic Properties and Contributions to Growth in Blood of the Meningococcal Haemoglobin Receptors, HpuAB and HmbR.Semantic proximity Read ↗

Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene.Semantic proximity Read ↗

HmbR outer membrane receptors of pathogenic Neisseria spp.: iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation.Semantic proximity Read ↗

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

Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in Neisseriae.Semantic proximity Read ↗

Analysis of TbpA and TbpB functionality in defective mutants of Neisseria meningitidis.Semantic proximity Read ↗

Iron piracy: acquisition of transferrin‐bound iron by bacterial pathogensSemantic proximity Read ↗

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

Analysis of haptoglobin and hemoglobin-haptoglobin interactions with the Neisseria meningitidis TonB-dependent receptor HpuAB by flow cytometry.Semantic proximity Read ↗

Monoclonal antibodies against the 70-kilodalton iron-regulated protein of Neisseria meningitidis are bactericidal and strain specificSemantic proximity Read ↗

Preparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB.Semantic proximity Read ↗

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