Evidence map›Paper›PMID 17438025›Full record

ArticleInfection and immunity2007

Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae.

Amanda J DeRocco, Cynthia Nau Cornelissen

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Clinical microbiology reviews · 2024
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Kinetic analysis of ligand interaction with the gonococcal transferrin-iron acquisition system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009
    Article
  12. Review
  13. 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

2 authors at 1 institution in 1 country.

Amanda J DeRoccoDepartment of Microbiology and Immunology, Virginia Commonwealth University Medical Center, Richmond, VA 23298-0678, USA.
Cynthia Nau Cornelissen
Virginia Commonwealth University Medical Center · US

Funding

Virus Vector Shared ResourceP30CA016059 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Keri R Maher · 1985 to 2026
$51.0M
A MOLECULAR STUDY OF THE GONOCOCCAL TRANSFERRIN RECEPTORR01AI047141 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CORNELISSEN, CYNTHIA N · 2001 to 2010
$3.1M
NCI NIH HHS P30 CA016059NCI NIH HHS P30 CA 16059NIAID NIH HHS R01 AI 047141NIAID NIH HHS R01 AI047141
6 · The paper itself

Abstract

The transferrin iron acquisition system of Neisseria gonorrhoeae is necessary for iron uptake from transferrin in the human host and requires the participation of two distinct proteins: TbpA and TbpB. TbpA is a TonB-dependent outer membrane transporter responsible for the transport of iron into the cell. TbpB is a lipid-modified protein, for which a precise role in receptor function has not yet been elucidated. These receptor complex proteins show promise as vaccine candidates; therefore, it is important to identify surface-exposed regions of the proteins required for wild-type functions. In this study we examined TbpB, which has been reported to be surface exposed in its entirety; however, this hypothesis has never been tested experimentally. We placed the hemagglutinin (HA) epitope into TbpB with the dual purpose of examining the surface exposure of particular epitopes as well as their impact on receptor function. Nine insertion mutants were created, placing the epitope downstream of the signal peptidase II cleavage site. We report that the HA epitope is surface accessible in all mutants, indicating that the full-length TbpB is completely surface exposed. By expressing the TbpB-HA fusion proteins in N. gonorrhoeae, we were able to examine the impact of each insertion on the function of TbpB and the transferrin acquisition process. We propose that TbpB is comprised of two transferrin-binding-competent lobes, both of which are critical for efficient iron uptake from human transferrin.

Indexed as

HemagglutininsRecombinant Fusion ProteinsTransferrin-Binding Protein BAmino Acid SequenceEpitopesHumansIronMicroscopy, ConfocalMolecular Sequence DataMutagenesis, InsertionalNeisseria gonorrhoeaeTransferrinEpitopesHemagglutininsIronRecombinant Fusion ProteinsTransferrinTransferrin-Binding Protein B

Identifiers

PMID17438025
PMCPMC1932913
OpenAlexW2116234046

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.