Evidence map›Paper›PMID 11083823›Full record

ArticleInfection and immunity2000

Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions.

I C Boulton, M K Yost, J E Anderson, C N Cornelissen

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

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  15. A structural comparison of human serum transferrin and human lactoferrin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2007
    Review
  16. Article
  17. Article
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  19. Iron transport systems in Neisseria meningitidis.Microbiology and molecular biology reviews : MMBR · 2004
    Review
  20. 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

4 authors at 2 institutions in 1 country.

I C BoultonDepartment of Microbiology and Immunology, Medical College of Virginia Campus of Virginia Commonwealth University, Richmond, Virginia 23298, USA.
M K Yost
J E Anderson
C N Cornelissen
Virginia Commonwealth University Medical Center · USUniversity of North Carolina at Chapel Hill · US

Funding

STRUCTURE OF THE GONOCOCCAL TRANSFERRIN RECEPTORR29AI039523 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CORNELISSEN, CYNTHIA NAU · 1996 to 2000
$107k
NIAID NIH HHS AI39523
6 · The paper itself

Abstract

The availability of free iron in vivo is strictly limited, in part by the iron-binding protein transferrin. The pathogenic Neisseria spp. can sequester iron from this protein, dependent upon two iron-repressible, transferrin-binding proteins (TbpA and TbpB). TbpA is a TonB-dependent, integral, outer membrane protein that may form a beta-barrel exposing multiple surface loops, some of which are likely to contain ligand-binding motifs. In this study we propose a topological model of gonococcal TbpA and then test some of the hypotheses set forth by the model by individually deleting three putative loops (designated loops 4, 5, and 8). Each mutant TbpA could be expressed without toxicity and was surface exposed as assessed by immunoblotting, transferrin binding, and protease accessibility. Deletion of loop 4 or loop 5 abolished transferrin binding to whole cells in solid- and liquid-phase assays, while deletion of loop 8 decreased the affinity of the receptor for transferrin without affecting the copy number. Strains expressing any of the three mutated TbpAs were incapable of growth on transferrin as a sole iron source. These data implicate putative loops 4 and 5 as critical determinants for receptor function and transferrin-iron uptake by gonococcal TbpA. The phenotype of the DeltaL8TbpA mutant suggests that high-affinity ligand interaction is required for transferrin-iron internalization.

Indexed as

Amino Acid SequenceBinding SitesCarrier ProteinsIronIron-Binding ProteinsMolecular Sequence DataMutationNeisseria gonorrhoeaeProtein ConformationTransferrinTransferrin-Binding ProteinsTrypsinCarrier ProteinsIronIron-Binding ProteinsTransferrinTransferrin-Binding ProteinsTrypsin

Identifiers

PMID11083823
PMCPMC97808
OpenAlexW2142122735

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.