Evidence map›Paper›PMID 22416675›Full record

ArticleBMC microbiology2012

Characterization of LysB4, an endolysin from the Bacillus cereus-infecting bacteriophage B4.

Bokyung Son, Jiae Yun, Jeong-A Lim, Hakdong Shin, Sunggi Heu, Sangryeol Ryu

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
7.4field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Biochemistry · 2025
    Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Lysins as a powerful alternative to combat Bacillus anthracis.Applied microbiology and biotechnology · 2024
    Review
  15. Article
  16. Engineered endolysin ofFrontiers in microbiology · 2024
    Article
  17. Article
  18. Isolation and Characterization of aJournal of microbiology and biotechnology · 2023
    Article
  19. Article
  20. Review

4 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Bokyung SonDepartment of Food and Animal Biotechnology, Seoul National University, Gwanak-gu, Seoul, Republic of Korea.
Jiae Yun
Jeong-A Lim
Hakdong Shin
Sunggi Heu
Sangryeol Ryu
Seoul National University · KRNational Academy of Agricultural Science · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBacillus cereus is a foodborne pathogen that causes emetic or diarrheal types of food poisoning. The incidence of B. cereus food poisoning has been gradually increasing over the past few years, therefore, biocontrol agents effective against B. cereus need to be developed. Endolysins are phage-encoded bacterial peptidoglycan hydrolases and have received considerable attention as promising antibacterial agents.

resultsThe endolysin from B. cereus phage B4, designated LysB4, was identified and characterized. In silico analysis revealed that this endolysin had the VanY domain at the N terminus as the catalytic domain, and the SH3_5 domain at the C terminus that appears to be the cell wall binding domain. Biochemical characterization of LysB4 enzymatic activity showed that it had optimal peptidoglycan hydrolase activity at pH 8.0-10.0 and 50°C. The lytic activity was dependent on divalent metal ions, especially Zn2+. The antimicrobial spectrum was relatively broad because LysB4 lysed Gram-positive bacteria such as B. cereus, Bacillus subtilis and Listeria monocytogenes and some Gram-negative bacteria when treated with EDTA. LC-MS analysis of the cell wall cleavage products showed that LysB4 was an L-alanoyl-D-glutamate endopeptidase, making LysB4 the first characterized endopeptidase of this type to target B. cereus.

conclusionsLysB4 is believed to be the first reported L-alanoyl-D-glutamate endopeptidase from B. cereus-infecting bacteriophages. The properties of LysB4 showed that this endolysin has strong lytic activity against a broad range of pathogenic bacteria, which makes LysB4 a good candidate as a biocontrol agent against B. cereus and other pathogenic bacteria.

Indexed as

Amino Acid SequenceBacillus cereusBacillus PhagesCatalytic DomainCations, DivalentCoenzymesComputational BiologyDNA, ViralEndopeptidasesEnzyme StabilityHydrogen-Ion ConcentrationMolecular Sequence DataN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanProtein Structure, TertiarySequence Analysis, DNACations, DivalentCoenzymesDNA, ViralendolysinEndopeptidasesN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanZinc

Identifiers

PMID22416675
PMCPMC3315420
OpenAlexW2031752327

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.