Evidence map›Paper›PMID 10986265›Full record

ArticleJournal of bacteriology2000

Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus.

P J Desai, E Garges, C A Genco

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.9field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Iron transport systems in Neisseria meningitidis.Microbiology and molecular biology reviews : MMBR · 2004
    Review
  5. Article
  6. Article
  7. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

P J DesaiThe Maxwell Finland Laboratory for Infectious Diseases, Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118, USA.
E Garges
C A Genco
Boston University · US

Funding

IRON ASSIMILATION BY PATHOGENIC NEISSERIA SPPR01AI030797 · NIAID · MOREHOUSE SCHOOL OF MEDICINE · PI GENCO, CAROLINE A · 1991 to 1995
–
HEME ASSIMILATION IN NGONORRHOEAER21AI030797 · NIAID · BOSTON MEDICAL CENTER · PI GENCO, CAROLINE A · 1998 to 1998
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NIAID NIH HHS AI30797
6 · The paper itself

Abstract

Redundant TonB systems which function in iron transport from TonB-dependent ligands have recently been identified in several gram-negative bacteria. We demonstrate here that in addition to the previously described tonB locus, an alternative system exists for the utilization of iron from hemoglobin, transferrin, or lactoferrin in Neisseria meningitidis and Neisseria gonorrhoeae. Following incubation on media containing hemoglobin, N. meningitidis IR3436 (tonB exbB exbD deletion mutant) and N. gonorrhoeae PD3401 (tonB insertional mutant) give rise to colonies which can grow with hemoglobin. Transfer of Hb(+) variants (PD3437 or PD3402) to media containing hemoglobin, transferrin, and/or lactoferrin as sole iron sources resulted in growth comparable to that observed for the wild-type strains. Transformation of N. meningitidis IR3436 or N. gonorrhoeae PD3401 with chromosomal DNA from the Hb(+) variants yielded transformants capable of growth with hemoglobin. When we inactivated the TonB-dependent outer membrane hemoglobin receptors (HmbR or HpuB) in the Neisseria Hb(+) variants, these strains could not grow with hemoglobin; however, growth was observed with transferrin and/or lactoferrin. These results demonstrate that accumulation of iron from hemoglobin, transferrin, and lactoferrin in the pathogenic neisseriae can occur via a system that is independent of the previously described tonB locus.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsHemoglobinsLactoferrinMembrane ProteinsMutagenesisNeisseria gonorrhoeaeNeisseria meningitidisReceptors, Cell SurfaceReceptors, TransferrinTransferrinTransformation, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsHemoglobinsHmbR protein, Neisseria meningitidisHpuB protein, NeisseriaLactoferrinMembrane ProteinsReceptors, Cell SurfaceReceptors, TransferrintonB protein, BacteriaTransferrin

Identifiers

PMID10986265
PMCPMC111005
OpenAlexW2117485739

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.