Evidence map›Paper›PMID 39724336›Full record

ArticleAMB Express2024

Characterization and bioinformatic analysis of a new chimeric endolysin against MRSA with great stability.

Sanaz Momen, Neda Soleimani, Farzaneh Azizmohseni, Yasaman Ahmadbeigi, Seddigheh Borhani, Zahra Amini-Bayat

Abstract read
In one paragraph

Article in AMB Express, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Biofilm formation and eradication ofIranian journal of microbiology · 2025
    Article
  5. 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.

Sanaz MomenDepartment of Microbiology and Microbial Biotechnology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran.
Neda SoleimaniDepartment of Microbiology and Microbial Biotechnology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran.
Farzaneh AzizmohseniDepartment of Biotechnology, Iranian Research Organization for Science and Technology (IROST), Tehran, Iran.
Yasaman AhmadbeigiDepartment of Microbiology and Microbial Biotechnology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran.
Seddigheh BorhaniBiophysics Department, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
Zahra Amini-BayatDepartment of Biotechnology, Iranian Research Organization for Science and Technology (IROST), Tehran, Iran. Amini-bayat@irost.org.ORCID http://orcid.org/0000-0003-2667-0486

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibiotics become less effective in treating infectious diseases as resistance increases. Staphylococcus aureus is a global problem due to its ability to form biofilms and resistance mechanisms. Phage endolysin is one of the most promising methods for combating antibiotic resistance. ZAM-MSC chimeric endolysin has three domains derived from SAL1 and lysostaphin, which target the peptide bridge of peptidoglycan. In this study purified ZAM-MSC (with yield of 30 mg/lit) had bactericidal activity against methicillin-sensitive Staphylococcus aureus (MSSA) and methicillin-resistant Staphylococcus aureus (MRSA) at low concentrations (2.38 μg/ml and 1.88 μg/ml, respectively). The antibacterial spectrum revealed that ZAM-MSC was active against diverse Staphylococci. it has maintained 100% stability after 24 h incubation in pH 5 to 10 against S. aureus, as well as demonstrated significant thermostability and maintained nearly its full activity at different temperatures (4-42 °C) up to 1 day of incubation. The anti-biofilm activity of various concentrations of ZAM-MSC against MSSA and MRSA biofilms was not dose-dependent, and antibiofilm activity was observed even at low concentrations (14 μg/ml). Further, the molecular dynamics simulations demonstrated that the ZAM-MSC chimer and its parent proteins remained dynamically stable, showing similar flexibility despite the size and hydrogen bond number differences. In conclusion, the study reveals that chimeric ZAM-MSC is a distinctive enzyme with exceptional biochemical properties and rapid lytic activity against Staphylococci.

Indexed as

Antibiotic resistanceBiofilmChimeric endolysinMRSAStaphylococcus aureus

Identifiers

PMID39724336
PMCPMC11671461

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.