Evidence map›Paper›PMID 37634214›Full record

ArticleThe protein journal2023

Staphylococcus aureus Bacteriophage 52 Endolysin Exhibits Anti-Biofilm and Broad Antibacterial Activity Against Gram-Positive Bacteria.

Mujib Abdulkadir Abdurahman, İnci Durukan, Tuba Dinçer, Serap Pektaş, Ersin Karataş, Ali Osman Kiliç

Abstract read
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In one paragraph

Article in The protein journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Biofilm formation and eradication ofIranian journal of microbiology · 2025
    Article
  6. Article
  7. Article
  8. Antibacterial activity of endolysin LysP70 fromFrontiers in microbiology · 2025
    Article
  9. Review
  10. Article
  11. 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

6 authors at 3 institutions in 2 countries.

Mujib Abdulkadir AbdurahmanDepartment of Medical Microbiology, Faculty of Medicine, Karadeniz Technical University, Trabzon, 61080, Turkey.ORCID http://orcid.org/0000-0001-6273-1536
İnci DurukanDepartment of Medical Microbiology, Faculty of Medicine, Karadeniz Technical University, Trabzon, 61080, Turkey.ORCID http://orcid.org/0000-0002-9789-4738
Tuba DinçerDepartment of Medical Biology, Faculty of Medicine, Karadeniz Technical University, Trabzon, Turkey.ORCID http://orcid.org/0000-0001-5054-168X
Serap PektaşDepartment of Chemistry, Faculty of Arts and Sciences, Recep Tayyip Erdogan University, Rize, Turkey.ORCID http://orcid.org/0000-0003-0497-6257
Ersin KarataşDepartment of Medical Services and Techniques, Patnos Vocational School, Ağrı İbrahim Çeçen University, Ağrı, Turkey.ORCID http://orcid.org/0000-0001-6848-7618
Ali Osman KiliçDepartment of Medical Microbiology, Faculty of Medicine, Karadeniz Technical University, Trabzon, 61080, Turkey. akilic@ktu.edu.tr.ORCID http://orcid.org/0000-0002-5506-0866
Karadeniz Technical University · TRAğrı İbrahim Çeçen University · TRRecep Tayyip Erdoğan University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteriophage endolysins have been shown to hold great promise as new antibacterial agents for animal and human health in food preservation. In the present study, endolysin from Staphylococcus aureus subsp. aureus ATCC 27692-B1 bacteriophage 52 (LysSA52) was cloned, expressed, and characterized for its antimicrobial properties. Following DNA extraction from bacteriophage 52, a 1446-bp DNA fragment containing the endolysin gene (lysSA52) was obtained by PCR amplification and cloned into pET SUMO expression vector. The positive clone was validated by sequencing and open-reading frame analysis. The LysSA52 sequence shared high homology with staphylococcal phage endolysins of the SA12, SA13, and DSW2 phages and others. The cloned lysSA52 gene encoding 481 amino acids endolysin was expressed in Escherichia coli BL21 with a calculated molecular mass of 66 kDa (LysSA52). This recombinant endolysin LysSA52 exhibited lytic activity against 8 of 10 Gram-positive bacteria via agar spot-on lawn antimicrobial assay, including methicillin-resistant Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus haemolyticus, Streptococcus pneumonia, Streptococcus pyogenes, Enterococcus faecium, Enterococcus faecalis, and Bacillus atrophaeus. In addition, the 0.50 mg/mL, LysSA52 endolysins reduced about 60% of the biofilms of S. aureus and S. epidermidis established on a microtiter plate in 12 h treatment. The data from this study indicate that LysSA52 endolysin could be used as an antibacterial protein to prevent and treat infections caused by staphylococci and several other Gram-positive pathogenic bacteria irrespective of their antibiotic resistance.

Indexed as

BacteriophagesMethicillin-Resistant Staphylococcus aureusStaphylococcal InfectionsAnimalsAnti-Bacterial AgentsEndopeptidasesHumansStaphylococcusStaphylococcus aureusAnti-Bacterial AgentsendolysinEndopeptidasesBacteriophageCloningEndolysinStaphylococcus

Identifiers

PMID37634214
OpenAlexW4386204044

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.