Evidence map›Paper›PMID 31319057›Full record

ArticleBiochimica et biophysica acta. Biomembranes2019

Modulation of antimicrobial potency of human cathelicidin peptides against the ESKAPE pathogens and in vivo efficacy in a murine catheter-associated biofilm model.

Jayaram Lakshmaiah Narayana, Biswajit Mishra, Tamara Lushnikova, Radha M Golla, Guangshun Wang

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2019. 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
3.7field-weighted citation impact, top 7% 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, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. 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

5 authors at 2 institutions in 1 country.

Jayaram Lakshmaiah NarayanaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, NE 68198-5900, USA.
Biswajit MishraDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, NE 68198-5900, USA.
Tamara LushnikovaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, NE 68198-5900, USA.
Radha M GollaDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, NE 68198-5900, USA.
Guangshun WangDepartment of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 985900 Nebraska Medical Center, Omaha, NE 68198-5900, USA. Electronic address: gwang@unmc.edu.
University of Nebraska Medical Center · USNebraska Medical Center · US

Funding

Database designed novel anti-MRSA peptidesR01AI105147 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, GUANGSHUN · 2015 to 2019
$1.9M
Database designed novel anti-MRSA peptidesR56AI105147 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, GUANGSHUN · 2013 to 2013
$354k
NIAID NIH HHS R01 AI105147NIAID NIH HHS R56 AI105147
6 · The paper itself

Abstract

Antimicrobial peptides are essential components of innate immune systems that protect hosts from infection. They are also useful candidates for developing a new generation of antibiotics to fight antibiotic-resistant pathogens. Human innate immune peptide LL-37 can inhibit biofilm formation, but suffers from high cost due to a long peptide length and rapid protease degradation. To improve the peptide, we previously identified the major active region and changed the peptide backbone structure. This study designed two families of new peptides by altering peptide side chains. Interestingly, these peptides displayed differential potency against various ESKAPE pathogens in vitro and substantially reduced hemolysis. Further potency test in vivo revealed that 17tF-W eliminated the burden of methicillin-resistant Staphylococcus aureus (MRSA) USA300 in both mouse-embedded catheters and their surrounding tissues. In addition, peptide treatment suppressed the level of chemokine TNFα, and boosted the levels of chemokines MCP-1, IL-17A and IL-10 in the surrounding tissues of the infected catheter embedded in mice. In conclusion, we have designed a set of new LL-37 peptides with varying antimicrobial activities, opening the door to potential topical treatment of infections involving different drug-resistant pathogens.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesBiofilmsCathelicidinsHumansMethicillin-Resistant Staphylococcus aureusMiceMicrobial Sensitivity TestsProtein EngineeringStaphylococcus aureusAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesCathelicidinsBiofilmsCathelicidinCatheterCytotoxicityLL-37Peptide design

Identifiers

PMID31319057
PMCPMC6689428
OpenAlexW2960441533

What OpenQuestion holds

Textmetadata
LicenceTDM
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.