Evidence map›Paper›PMID 9733695›Full record

ArticleJournal of bacteriology1998

YscB of Yersinia pestis functions as a specific chaperone for YopN.

M W Jackson, J B Day, G V Plano

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  3. Chromosomally-EncodedFrontiers in cellular and infection microbiology · 2019
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  11. 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.

M W JacksonDepartment of Microbiology and Immunology, University of Miami School of Medicine, Miami, Florida 33176, USA.
J B Day
G V Plano
University of Miami · US

Funding

Control of virulence protein export in Yersinia pestisR01AI039575 · NIAID · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI PLANO, GREGORY V · 2001 to 2011
$3.3M
CONTROL OF VIRULENCE PROTEIN EXPORT IN YERSINIA PESTISR29AI039575 · NIAID · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI PLANO, GREGORY V · 1996 to 2000
$112k
NIAID NIH HHS AI39575NIAID NIH HHS R01 AI039575NIAID NIH HHS R29 AI039575
6 · The paper itself

Abstract

Following contact with a eucaryotic cell, Yersinia species pathogenic for humans (Y. pestis, Y. pseudotuberculosis, and Y. enterocolitica) export and translocate a distinct set of virulence proteins (YopE, YopH, YopJ, YopM, and YpkA) from the bacterium into the eucaryotic cell. During in vitro growth at 37 degrees C in the presence of calcium, Yop secretion is blocked; however, in the absence of calcium, Yop secretion is triggered. Yop secretion occurs via a plasmid-encoded type III, or "contact-dependent," secretion system. The secreted YopN (also known as LcrE), TyeA, and LcrG proteins are necessary to prevent Yop secretion in the presence of calcium and prior to contact with a eucaryotic cell. In this paper we characterize the role of the yscB gene product in the regulation of Yop secretion in Y. pestis. A yscB deletion mutant secreted YopM and V antigen both in the presence and in the absence of calcium; however, the export of YopN was specifically reduced in this strain. Complementation with a functional copy of yscB in trans completely restored the wild-type secretion phenotype for YopM, YopN, and V antigen. The YscB amino acid sequence showed significant similarities to those of SycE and SycH, the specific Yop chaperones for YopE and YopH, respectively. Protein cross-linking and immunoprecipitation studies demonstrated a specific interaction between YscB and YopN. In-frame deletions in yopN eliminating the coding region for amino acids 51 to 85 or 6 to 100 prevented the interaction of YopN with YscB. Taken together, these results indicate that YscB functions as a specific chaperone for YopN in Y. pestis.

Indexed as

Membrane ProteinsAmino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsBinding SitesMolecular ChaperonesMolecular Sequence DataMutationTrans-ActivatorsYersinia pestisBacterial Outer Membrane ProteinsBacterial ProteinsMembrane ProteinsMolecular ChaperonesSycE protein, YersiniaTrans-ActivatorsyopE protein, YersiniaYopN protein, Yersinia

Identifiers

PMID9733695
PMCPMC107517
OpenAlexW2154675618

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.