Evidence map›Paper›PMID 19398546›Full record

ArticleInfection and immunity2009

The metal homeostasis protein, Lsp, of Streptococcus pyogenes is necessary for acquisition of zinc and virulence.

Benjamin F Weston, Audrey Brenot, Michael G Caparon

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 65 citations in OpenAlex.

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  16. Iron and zinc exploitation during bacterial pathogenesis.Metallomics : integrated biometal science · 2015
    Review
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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.

Benjamin F WestonDepartment of Molecular Microbiology, Washington University School of Medicine, St Louis, Missouri 63110-1093, USA.
Audrey Brenot
Michael G Caparon
Washington University in St. Louis · US

Funding

PROTEASE AND ROP GENES IN S. PYOGENES VIRULENCER01AI046433 · NIAID · WASHINGTON UNIVERSITY · PI CAPARON, MICHAEL G. · 2000 to 2014
$4.7M
Novel Catabolite Repression Pathway Controls Virulence in Streptococcus pyogenesR01AI070759 · NIAID · WASHINGTON UNIVERSITY · PI CAPARON, MICHAEL G. · 2007 to 2018
$3.4M
Cytolysin-mediated translocation in S.pyogenes virulenceR01AI064721 · NIAID · WASHINGTON UNIVERSITY · PI CAPARON, MICHAEL G. · 2005 to 2014
$3.3M
MECHANISMS OF CHILDHOOD INFECTION AND IMMUNITYT32HD007507 · NICHD · WASHINGTON UNIVERSITY · PI STORCH, GREGORY A. · 1998 to 2007
$1.7M
NIAID NIH HHS AI046433NIAID NIH HHS AI064721NIAID NIH HHS AI070759NIAID NIH HHS R01 AI046433NIAID NIH HHS R01 AI064721NIAID NIH HHS R01 AI070759NICHD NIH HHS 5T32HD007507-10NICHD NIH HHS T32 HD007507
6 · The paper itself

Abstract

"Cluster 9" family lipoproteins function as ligand-binding subunits of ABC-type transporters in maintaining transition metal homeostasis and have been implicated in the virulence of several bacteria. While these proteins share high similarity, the specific metal that they recognize and whether their role in virulence directly involves metal homeostasis cannot be reliably predicted. We examined the cluster 9 protein Lsp of Streptococcus pyogenes and found that specific deletion of lsp produced mutants highly attenuated in a murine model of soft tissue infection. Under standard in vitro conditions, growth of the Lsp(-) mutant was indistinguishable from that of the wild type, but growth was defective under zinc-limited conditions. The growth defect could be complemented by plasmids expressing wild-type Lsp but not Lsp engineered to lack its putative lipidation residue. Furthermore, Zn(2+) but not Mn(2+) rescued Lsp(-) growth, implicating Zn(2+) as the physiological ligand for Lsp. Mutation of residues in the putative Zn(2+)-binding pocket generated variants both hypo- and hyper-resistant to zinc starvation, and both mutant classes displayed attenuated virulence. Together, these data suggest that Lsp is a ligand-binding component of an ABC-type zinc permease and that perturbation of zinc homeostasis inhibits the ability of S. pyogenes to cause disease in a zinc-limited host milieu.

Indexed as

AnimalsATP-Binding Cassette TransportersBinding SitesGene DeletionGenetic Complementation TestManganeseMiceMutagenesis, Site-DirectedMutation, MissenseSoft Tissue InfectionsStreptococcal InfectionsStreptococcus pyogenesVirulenceVirulence FactorsZincATP-Binding Cassette TransportersManganeseVirulence FactorsZinc

Identifiers

PMID19398546
PMCPMC2708593
OpenAlexW2112911356

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.