Evidence map›Paper›PMID 27895129›Full record

ArticleInfection and immunity2017

The Predicted Lytic Transglycosylase HpaH from Xanthomonas campestris pv. vesicatoria Associates with the Type III Secretion System and Promotes Effector Protein Translocation.

Jens Hausner, Nadine Hartmann, Michael Jordan, Daniela Büttner

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
7.5field-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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Measure of Peptidoglycan Degradation Activity.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Jens HausnerInstitute of Biology, Genetics Department, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Nadine HartmannInstitute of Biology, Genetics Department, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Michael JordanInstitute of Biology, Genetics Department, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Daniela BüttnerInstitute of Biology, Genetics Department, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany daniela.buettner@genetik.uni-halle.de.
Martin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pathogenicity of the Gram-negative plant-pathogenic bacterium Xanthomonas campestris pv. vesicatoria depends on a type III secretion (T3S) system, which spans both bacterial membranes and translocates effector proteins into plant cells. The assembly of the T3S system presumably involves the predicted lytic transglycosylase (LT) HpaH, which is encoded adjacent to the T3S gene cluster. Bacterial LTs degrade peptidoglycan and often promote the formation of membrane-spanning macromolecular protein complexes. In the present study, we show that HpaH localizes to the bacterial periplasm and binds to peptidoglycan as well as to components of the T3S system, including the predicted periplasmic inner rod proteins HrpB1 and HrpB2 as well as the pilus protein HrpE. In vivo translocation assays revealed that HpaH promotes the translocation of various effector proteins and of early substrates of the T3S system, suggesting a general contribution of HpaH to type III-dependent protein export. Mutant studies and the analysis of reporter fusions showed that the N-terminal region of HpaH contributes to protein function and is proteolytically cleaved. The N-terminally truncated HpaH cleavage product is secreted into the extracellular milieu by a yet-unknown transport pathway, which is independent of the T3S system.

Indexed as

Type III Secretion SystemsAmino Acid SequenceBacterial ProteinsBase SequenceCodon, InitiatorGene ExpressionGene Expression Regulation, BacterialModels, MolecularMolecular ConformationPeptidoglycanPeptidoglycan GlycosyltransferasePlantsProtein BindingProtein BiosynthesisProtein Interaction Domains and MotifsProtein TransportBacterial ProteinsCodon, InitiatorPeptidoglycanPeptidoglycan GlycosyltransferaseRecombinant Fusion ProteinsType III Secretion Systemseffector proteinslytic transglycosylasepeptidoglycanSlt70type III secretionXanthomonas

Identifiers

PMID27895129
PMCPMC5278175
OpenAlexW2559571174

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.