Evidence map›Paper›PMID 34878337›Full record

ArticleMicrobiology spectrum2021

Design SMAP29-LysPA26 as a Highly Efficient Artilysin against Pseudomonas aeruginosa with Bactericidal and Antibiofilm Activity.

Tingting Wang, Yongxiang Zheng, Jiami Dai, Junxiu Zhou, Rong Yu, Chun Zhang

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. UnderstandingMicroorganisms · 2026
    Review
  5. Review
  6. Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. CombatingFrontiers in cellular and infection microbiology · 2025
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
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 1 institution in 1 country.

Tingting Wang *Department of Biopharmaceutics, West China School of Pharmacy, Sichuan University, Chengdu, China.
Yongxiang Zheng *Department of Biopharmaceutics, West China School of Pharmacy, Sichuan University, Chengdu, China.
Jiami DaiDepartment of Biopharmaceutics, West China School of Pharmacy, Sichuan University, Chengdu, China.
Junxiu ZhouDepartment of Biopharmaceutics, West China School of Pharmacy, Sichuan University, Chengdu, China.
Rong YuDepartment of Biopharmaceutics, West China School of Pharmacy, Sichuan University, Chengdu, China.
Chun ZhangDepartment of Biopharmaceutics, West China School of Pharmacy, Sichuan University, Chengdu, China.ORCID 0000-0002-4646-1879
Sichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial resistance (AMR) is a major issue to global health. The multidrug-resistant (MDR) Gram-negative infections, particularly infected by carbapenem-resistant pathogens, urgently need efficient antibiotics and novel therapy. However, the scientific challenges of aiming for innovative approaches against Gram-negative bacteria have hindered the research and development of antibiotic drugs. Phage-derived endolysins are bacteriolytic and specific for a bacterial species or genus, providing a promising antibiotic strategy. However, the outer membrane of Gram-negative bacteria could prevent the peptidoglycan layer from the hydrolysis of endolysins. Antimicrobial peptides usually destabilize the outer membrane and could enhance the antibiotic activity of endolysins. In this study, we designed new artilysins with antimicrobial-peptide SMAP29 fusion at the N-terminal of LysPA26 (named as AL-3AA, AL-9AA, and AL-15AA), and evaluated them. The results showed artilysin AL-3AA to be highly bactericidal; even 0.05 mg/mL AL-3AA could reduce 5.81 log units P. aeruginosa without EDTA in 60 min. It killed P. aeruginosa rapidly and dose-dependently through cell lysis. AL-3AA inhibited P. aeruginosa PAO1 biofilm formation and significantly decreased mature P. aeruginosa biofilms. It also had potential broad-spectrum activity against susceptible Gram-negative bacteria in the hospital, including K. pneumoniae and E. coli. The antibacterial mechanism investigation has provided valuable information about the antibacterial action of AL-3AA, which can lyse and disintegrate the bacterial quickly. These results suggested AL-3AA could be a new and promising antimicrobial agent for the combat of P. aeruginosa.

Indexed as

Anti-Bacterial AgentsAntimicrobial PeptidesBiofilmsDrug DesignEscherichia coliHumansKlebsiella pneumoniaeMicrobial Sensitivity TestsPseudomonas aeruginosaPseudomonas InfectionsAnti-Bacterial AgentsAntimicrobial PeptidesAL-3AAantimicrobial agentantimicrobial resistancebactericidalbiofilmcircular dichroismendolysinGram-negative infectionLysPA26protein designPseudomonas aeruginosaSMAP29

Identifiers

PMID34878337
PMCPMC8653812
OpenAlexW4200398189

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.