Evidence map›Paper›PMID 11371518›Full record

ArticleJournal of bacteriology2001

HreP, an in vivo-expressed protease of Yersinia enterocolitica, is a new member of the family of subtilisin/kexin-like proteases.

G Heusipp, G M Young, V L Miller

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

9 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Characteristics of Yersinia enterocolitica biotype 1A strains isolated from patients and asymptomatic carriers.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2013
    Article
  3. Article
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  5. Article
  6. 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.

G HeusippDepartment of Molecular Microbiology, Washington University School of Medicine and St. Louis Children's Hospital, St. Louis, Missouri 63110, USA.
G M Young
V L Miller
St. Louis Children's Hospital · US

Funding

NOVEL VIRULENCE GENES OF YERSINIAR01AI042736 · NIAID · WASHINGTON UNIVERSITY · PI MILLER, VIRGINIA L · 1999 to 2003
$1.2M
NIAID NIH HHS AI42736
6 · The paper itself

Abstract

The role of proteases in pathogenesis is well established for several microorganisms but has not been described for Yersinia enterocolitica. Previously, we identified a gene, hreP, which showed significant similarity to proteases in a screen for chromosomal genes of Y. enterocolitica that were exclusively expressed during an infection of mice. We cloned this gene by chromosome capture and subsequently determined its nucleotide sequence. Like inv, the gene encoding the invasin protein of Y. enterocolitica, hreP is located in a cluster of flagellum biosynthesis and chemotaxis genes. The genomic organization of this chromosomal region is different in Escherichia coli, Salmonella, and Yersinia pestis than in Y. enterocolitica. Analysis of the distribution of hreP between different Yersinia isolates and the relatively low G+C content of the gene suggests acquisition by horizontal gene transfer. Sequence analysis also revealed that HreP belongs to a family of eukaryotic subtilisin/kexin-like proteases. Together with the calcium-dependent protease PrcA of Anabaena variabilis, HreP forms a new subfamily of bacterial subtilisin/kexin-like proteases which might have originated from a common eukaryotic ancestor. Like other proteases of this family, HreP is expressed with an N-terminal prosequence. Expression of an HreP-His(6) tag fusion protein in E. coli revealed that HreP undergoes autocatalytic processing at a consensus cleavage site of subtilisin/kexin-like proteases, thereby releasing the proprotein.

Indexed as

Bacterial ProteinsGenome, BacterialProprotein ConvertasesSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase CompositionBlotting, SouthernBlotting, WesternCloning, MolecularEscherichia coliGene Transfer, HorizontalMolecular Sequence DataProtein Processing, Post-TranslationalSequence Analysis, DNASequence Homology, Amino AcidSubtilisinsBacterial ProteinsHreP protein, Yersinia enterocoliticaKEX2 protein, S cerevisiaePrcA protein, bacteriaProprotein ConvertasesSaccharomyces cerevisiae ProteinsSubtilisins

Identifiers

PMID11371518
PMCPMC95231
OpenAlexW1965257500

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.