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

Phase variation of hemoglobin utilization in Neisseria gonorrhoeae.

Infection and immunity - 1 Mar 1998

Chen C J, Elkins C, Sparling P F

Abstract excerpt

Most Neisseria gonorrhoeae isolates are unable to use human hemoglobin as the sole source of iron for growth (Hgb-), but a minor population is able to do so (Hgb+). This minor population grows luxuriously on hemoglobin, expresses two outer membrane proteins of 42 kDa (HpuA) and 89 kDa (HpuB), and binds hemoglobin under iron-stressed conditions. In addition to the previously reported HpuB, we identified and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Outer Membrane Proteins
Share to Blotting, Southern

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

Share to Genes, Bacterial

Share to Hemoglobins

Share to Molecular Sequence Data

Share to Mutation

Share to Polymerase Chain Reaction

Source

Open in PubMed Open full text

Identifiers

PMID: 9488386
DOI: 10.1128/IAI.66.3.987-993.1998
PMCID: PMC108006

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phase variation of hemoglobin utilization in Neisseria gonorrhoeae.PMID 9488386Read ↗

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

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

HmbR, a hemoglobin-binding outer membrane protein of Neisseria meningitidis, undergoes phase variation.Semantic proximity Read ↗

Neisseria gonorrhoeae heme biosynthetic mutants utilize heme and hemoglobin as a heme source but fail to grow within epithelial cells.Semantic proximity Read ↗

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

Genotypic and phenotypic modifications of Neisseria meningitidis after an accidental human passage.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 ↗

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

Questions about gonococcal pilus phase‐ and antigenic variationSemantic proximity Read ↗

The distribution and 'in vivo' phase variation status of haemoglobin receptors in invasive meningococcal serogroup B disease: genotypic and phenotypic analysis.Semantic proximity Read ↗

Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes.Semantic proximity Read ↗

A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds.Semantic proximity Read ↗

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