Evidence map›Paper›PMID 28912099›Full record

ArticleBiochimica et biophysica acta. Biomembranes2017

Antimicrobial peptides are degraded by the cytosolic proteases of human erythrocytes.

Charles G Starr, William C Wimley

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 101 citations in OpenAlex.

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  12. Modulating Antimicrobial Activity and Structure of the Peptide Esc(1-21) via Site-Specific Isopeptide Bond Formation.Journal of peptide science : an official publication of the European Peptide Society · 2025
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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

2 authors at 1 institution in 1 country.

Charles G StarrDepartment of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, LA 70112, USA.
William C WimleyDepartment of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, LA 70112, USA. Electronic address: wwimley@tulane.edu.
Tulane University · US

Funding

Molecular evolution of Peptide antibiotics for drug-resistant Gram negative bacteriaR21AI119104 · NIAID · TULANE UNIVERSITY OF LOUISIANA · PI WIMLEY, WILLIAM C · 2015 to 2016
$405k
NIAID NIH HHS R21 AI119104
6 · The paper itself

Abstract

Well-studied and promising antimicrobial peptides (AMPs), with potent bactericidal activity, in vitro, have yet to have a significant impact in human medicine beyond topical applications. We previously showed that interactions of AMPs with concentrated human erythrocytes inhibit many of them, and suggested that screens and assays should be done in their presence to mimic host cell inhibition. Here, we use AMPs to characterize the activity of proteases that are associated with human erythrocytes. The representative AMPs, ARVA and indolicidin, are degraded significantly during incubation with dilute, washed erythrocytes and yield a variety of degradation products, suggesting significant exopeptidase activity. Comparison of these fragments with those obtained from incubation with serum shows that the proteolytic activity associated with cells yields unique products that are not explained by residual serum proteases. By separately testing the membrane and cytosolic fractions, we show that erythrocyte proteolytic activity is found only in the cytosol. Finally, we incubated a diverse cross-section of natural and synthetic linear AMPs with human erythrocyte cytosolic extracts and observed degradation of all of them. These results show that, in addition to cell binding, proteolysis can also contribute significantly to host cell inhibition of AMPs in vitro and possibly also in vivo.

Indexed as

Amino Acid SequenceAntimicrobial Cationic PeptidesCytosolErythrocytesExopeptidasesHumansKineticsPeptide FragmentsProteolysisAntimicrobial Cationic PeptidesExopeptidasesPeptide FragmentsAntibioticPeptidaseProteolysisRed blood cell

Identifiers

PMID28912099
PMCPMC5659893
OpenAlexW2755572508

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.