Evidence map›Paper›PMID 20199604›Full record

ArticleMolecular microbiology2010

A dominant-negative needle mutant blocks type III secretion of early but not late substrates in Yersinia.

Alison J Davis, Dennise A De Jesús Díaz, Joan Mecsas

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  7. Regulation of the Yersinia type III secretion system: traffic control.Frontiers in cellular and infection microbiology · 2013
    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.

Alison J DavisDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. Alison_J.Davis@tufts.edu
Dennise A De Jesús Díaz
Joan Mecsas
Tufts University · US

Funding

Building Diversity in Biomedical SciencesR25HL007785 · NHLBI · TUFTS UNIVERSITY BOSTON · PI MAGUIRE, JAMIE LYNN · 2008 to 2024
$2.0M
Yersinia Yops in an Animal Infection ModelR01AI056068 · NIAID · TUFTS UNIVERSITY BOSTON · PI MECSAS, JOAN C. · 2003 to 2007
$1.8M
SHORT-TERM TRAINING FOR MINORITY STUDENTS PROGRAMT35HL007785 · NHLBI · TUFTS UNIVERSITY BOSTON · PI MECSAS, JOAN C. · 1993 to 2007
$829k
Inhibitors of Type III Secretion and Translocation in yersiniaR56AI073759 · NIAID · TUFTS UNIVERSITY BOSTON · PI MECSAS, JOAN C · 2008 to 2009
$824k
Role of the Y. pseudotuberculosis YscF protein in toxin delivery into host cellsK01DK075720 · NIDDK · TUFTS UNIVERSITY BOSTON · PI DAVIS, ALISON J · 2007 to 2011
$603k
NHLBI NIH HHS HL007785NHLBI NIH HHS R25 HL007785NHLBI NIH HHS T35 HL007785NIAID NIH HHS AI056068NIAID NIH HHS AI073759NIAID NIH HHS R01 AI056068NIAID NIH HHS R56 AI073759NIDDK NIH HHS DK075720NIDDK NIH HHS K01 DK075720
6 · The paper itself

Abstract

Yersinia pseudotuberculosis uses a type III secretion system (T3SS) to deliver effectors into host cells. A key component of the T3SS is the needle, which is a hollow tube on the bacterial surface through which effectors are secreted, composed of the YscF protein. To study needle assembly, we performed a screen for dominant-negative yscF alleles that prevented effector secretion in the presence of wild-type (WT) YscF. One allele, yscF-L54V, prevents WT YscF secretion and needle assembly, although purified YscF-L54V polymerizes in vitro. YscF-L54V binds to its chaperones YscE and YscG, and the YscF-L54V-EG complex targets to the T3SS ATPase, YscN. We propose that YscF-L54V stalls at a binding site in the needle assembly pathway following its release from the chaperones, which blocks the secretion of WT YscF and other early substrates required for building a needle. Interestingly, YscF-L54V does not affect the activity of pre-assembled actively secreting machines, indicating that a factor and/or binding site required for YscF secretion is absent from T3SS machines already engaged in effector secretion. Thus, substrate switching may involve the removal of an early substrate-specific binding site as a mechanism to exclude early substrates from Yop-secreting machines.

Indexed as

Mutation, MissenseAmino Acid SubstitutionBacterial ProteinsMacromolecular SubstancesMembrane ProteinsMembrane Transport ProteinsModels, MolecularMolecular ChaperonesProtein MultimerizationProtein Structure, TertiaryVirulence FactorsYersinia pseudotuberculosisBacterial ProteinsMacromolecular SubstancesMembrane ProteinsMembrane Transport ProteinsMolecular ChaperonesVirulence FactorsYscG protein, Yersinia

Identifiers

PMID20199604
PMCPMC2911021
OpenAlexW2000297455

What OpenQuestion holds

Textmetadata
LicenceTDM
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.