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

Monoclonal antibodies against the 70-kilodalton iron-regulated protein of Neisseria meningitidis are bactericidal and strain specific

1 Sept 1990

Abstract excerpt

When grown under iron limitation, Neisseria meningitidis expresses a number of outer membrane proteins (OMPs), one of which is a 70-kilodalton (kDa) major OMP. After immunization of mice with outer membrane preparations of iron-depleted cells of strain H44/76 (B:15:P1.7,16), hybridoma cell lines producing monoclonal antibodies against the 70-kDa OMP were obtained. Some of these monoclonal antibodies demonstrated...

Read the complete abstract on PubMed

Topics

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

Share to Antibiotic Resistance in Bacteria
Share to Bacterial Infections and Vaccines
Share to Pneumonia and Respiratory Infections

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

Source

Identifiers

PMID: 1696939
DOI: 10.1128/iai.58.9.3036-3041.1990

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

Monoclonal antibodies against the 70-kilodalton iron-regulated protein of Neisseria meningitidis are bactericidal and strain specificPMID 1696939Read ↗

Induction of immune responses by purified outer membrane protein complexes from Neisseria meningitidis.Semantic proximity Read ↗

Sequence variability of FrpB, a major iron-regulated outer-membrane protein in the pathogenic neisseriae.Semantic proximity Read ↗

Molecular characterization of FrpB, the 70-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis.Semantic proximity Read ↗

Evaluation of recombinant transferrin-binding protein B variants from Neisseria meningitidis for their ability to induce cross-reactive and bactericidal antibodies against a genetically diverse collection of serogroup B strains.Semantic proximity Read ↗

Towards the Immunoproteome of Neisseria meningitidisSemantic proximity Read ↗

Expression of the L8 lipopolysaccharide determinant increases the sensitivity of Neisseria meningitidis to serum bactericidal activity.Semantic proximity Read ↗

Protective Activity of Monoclonal Antibodies to Genome-Derived Neisserial Antigen 1870, a Neisseria meningitidis Candidate VaccineSemantic proximity Read ↗

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

Inactivation of the Moraxella catarrhalis 7169 Ferric Uptake Regulator Increases Susceptibility to the Bactericidal Activity of Normal Human SeraSemantic proximity Read ↗

Variation of the factor H-binding protein of Neisseria meningitidis.Semantic proximity Read ↗

Immunoproteomic identification of the hypothetical protein NMB1468 as a novel lipoprotein ubiquitous in <b><i>Neisseria meningitidis</i></b> with vaccine potentialSemantic proximity Read ↗

Specificity of human bactericidal antibodies against PorA P1.7,16 induced with a hexavalent meningococcal outer membrane vesicle vaccineSemantic proximity Read ↗

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