Evidence map›Paper›PMID 20971910›Full record

ArticleJournal of bacteriology2011

In vitro studies of peptidoglycan binding and hydrolysis by the Bacillus anthracis germination-specific lytic enzyme SleB.

Jared D Heffron, Nora Sherry, David L Popham

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Journal of biological chemistry · 2018
    Article
  10. Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Bacterial cell-wall recycling.Annals of the New York Academy of Sciences · 2013
    Review
  20. 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

3 authors at 1 institution in 1 country.

Jared D HeffronDepartment of Biological Sciences, Virginia Tech, Blacksburg, Virginia 24061, USA.
Nora Sherry
David L Popham
Virginia Tech · US

Funding

SPORE PEPTIDOGLYCAN DEGRADATION IN BACILLUS ANTHRACISR21AI060726 · NIAID · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI POPHAM, DAVID L · 2004 to 2005
$492k
NIAID NIH HHS AI060726NIAID NIH HHS R21 AI060726
6 · The paper itself

Abstract

The Bacillus anthracis endospore loses resistance properties during germination when its cortex peptidoglycan is degraded by germination-specific lytic enzymes (GSLEs). Although this event normally employs several GSLEs for complete cortex removal, the SleB protein alone can facilitate enough cortex hydrolysis to produce vulnerable spores. As a means to better understand its enzymatic function, SleB was overexpressed, purified, and tested in vitro for depolymerization of cortex by measurement of optical density loss and the solubilization of substrate. Its ability to bind peptidoglycan was also investigated. SleB functions independently as a lytic transglycosylase on both intact and fragmented cortex. Most of the muropeptide products that SleB generates are large and are potential substrates for other GSLEs present in the spore. Study of a truncated protein revealed that SleB has two domains. The N-terminal domain is required for stable peptidoglycan binding, while the C-terminal domain is the region of peptidoglycan hydrolytic activity. The C-terminal domain also exhibits dependence on cortex containing muramic-δ-lactam in order to carry out hydrolysis. As the conditions and limitations for SleB activity are further elucidated, they will enable the development of treatments that stimulate premature germination of B. anthracis spores, greatly simplifying decontamination measures.

Indexed as

AmidohydrolasesBacillus anthracisBacterial ProteinsGene Expression Regulation, BacterialHydrolysisLactamsMuramic AcidsPeptidoglycanProtein BindingProtein ConformationAmidohydrolasesBacterial ProteinsLactamsMuramic AcidsPeptidoglycanSleB protein, Bacillus

Identifiers

PMID20971910
PMCPMC3019929
OpenAlexW2143398237

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.