Evidence map›Paper›PMID 27542832›Full record

ArticleBMC microbiology2016

Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii.

Stephanie M Barksdale, Evelyn J Hrifko, Ezra Myung-Chul Chung, Monique L van Hoek

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Anti-Frontiers in microbiology · 2023
    Review
  6. Review
  7. Article
  8. Machine Learning Prediction of Antimicrobial Peptides.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Article
  10. Frontiers in microbiology · 2021
    Article
  11. Article
  12. Article
  13. Deimination Protein Profiles inFrontiers in immunology · 2020
    Article
  14. Article
  15. Article
  16. Biology ofFrontiers in cellular and infection microbiology · 2017
    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

4 authors at 1 institution in 1 country.

Stephanie M BarksdaleSchool of Systems Biology, George Mason University, Manassas, VA, USA.
Evelyn J HrifkoCollege of Science, George Mason University, Manassas, VA, USA.
Ezra Myung-Chul ChungNational Center of Biodefense and Infectious Diseases, George Mason University, 10920 George Mason Cir, 10920 George Mason Circle, MSN 1H8, Manassas, VA, 20110, USA.
Monique L van HoekSchool of Systems Biology, George Mason University, Manassas, VA, USA. mvanhoek@gmu.edu.
George Mason University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundOur group has developed a new process for isolating and identifying novel cationic antimicrobial peptides from small amounts of biological samples. Previously, we identified several active antimicrobial peptides from 100 μl of plasma from Alligator mississippiensis. These peptides were found to have in vitro antimicrobial activity against Pseudomonas aeruginosa and Staphylococcus aureus. In this work, we further characterize three of the novel peptides discovered using this process: Apo5, Apo6, and A1P.

resultsWe examined the activity of these peptides against multi-drug resistant strains and clinical isolates of common human pathogens. We investigated their structural characteristics using circular dichroism and tested for membrane disruption and DNA binding. These peptides were found to have strong in vitro activity against multi-drug resistant and clinically isolated strains of S. aureus, Escherichia coli, P. aeruginosa, and Acinetobacter baumannii. Apo5 and Apo6, peptides derived from alligator apolipoprotein C-1, depolarized the bacterial membrane. A1P, a peptide from the serpin proteinase inhibitor, did not permeabilize membranes. Performing circular dichroism analysis, Apo5 and Apo6 were found to be predominantly helical in SDS and TFE buffer, while A1P has significantly different structures in phosphate buffer, SDS, and TFE. None of these peptides were found to be hemolytic to sheep red blood cells or significantly cytotoxic up to 100 μg/ml after 24 h exposure.

conclusionsOverall, we suggest that Apo5 and Apo6 have a different mode of action than A1P, and that all three peptides make promising candidates for the treatment of drug-resistant bacteria, such as A. baumannii.

Indexed as

Acinetobacter baumanniiAlligators and CrocodilesAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCell MembraneDrug Resistance, Multiple, BacterialErythrocytesEscherichia coliMicrobial Sensitivity TestsProtein Structure, SecondaryProtein Structure, TertiaryPseudomonas aeruginosaSheepStaphylococcus aureusAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAcinetobacter baumanniiAlligator mississippiensisAntimicrobial peptidesEscherichia coliMulti-drug resistant bacteriaStaphylococcus aureus

Identifiers

PMID27542832
PMCPMC4992317
OpenAlexW2512827376

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.