Evidence map›Paper›PMID 20713107›Full record

ArticlePeptides2010

Cost-effective expression and purification of antimicrobial and host defense peptides in Escherichia coli.

B Bommarius, H Jenssen, M Elliott, J Kindrachuk, Mukesh Pasupuleti, H Gieren, K-E Jaeger, R E W Hancock, D Kalman

Abstract read
In one paragraph

Article in Peptides, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed.

  1. Review
  2. Multicopy Expression of the Marine Antimicrobial Peptide SpgillcinProbiotics and antimicrobial proteins · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Frontiers in bioengineering and biotechnology · 2023
    Article
  14. The future of recombinant host defense peptides.Microbial cell factories · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Nitric oxide-secreting probiotics as sustainable bio-cleaners for reverse osmosis membrane systems.Environmental science and pollution research international · 2022
    Review
  20. Article

1 more citing papers are in PubMed but not listed here.

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

9 authors.

B BommariusDepartment of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322, USA.
H Jenssen
M Elliott
J Kindrachuk
Mukesh Pasupuleti
H Gieren
K-E Jaeger
R E W Hancock
D Kalman

Funding

Mechanisms of pox virus motility and releaseR01AI072462 · NIAID · EMORY UNIVERSITY · PI KALMAN, DANIEL · 2008 to 2012
$2.2M
CIHRNIAID NIH HHS R01 AI072462
6 · The paper itself

Abstract

Cationic antimicrobial host defense peptides (HDPs) combat infection by directly killing a wide variety of microbes, and/or modulating host immunity. HDPs have great therapeutic potential against antibiotic-resistant bacteria, viruses and even parasites, but there are substantial roadblocks to their therapeutic application. High manufacturing costs associated with amino acid precursors have limited the delivery of inexpensive therapeutics through industrial-scale chemical synthesis. Conversely, the production of peptides in bacteria by recombinant DNA technology has been impeded by the antimicrobial activity of these peptides and their susceptibility to proteolytic degradation, while subsequent purification of recombinant peptides often requires multiple steps and has not been cost-effective. Here we have developed methodologies appropriate for large-scale industrial production of HDPs; in particular, we describe (i) a method, using fusions to SUMO, for producing high yields of intact recombinant HDPs in bacteria without significant toxicity and (ii) a simplified 2-step purification method appropriate for industrial use. We have used this method to produce seven HDPs to date (IDR1, MX226, LL37, CRAMP, HHC-10, E5 and E6). Using this technology, pilot-scale fermentation (10L) was performed to produce large quantities of biologically active cationic peptides. Together, these data indicate that this new method represents a cost-effective means to enable commercial enterprises to produce HDPs in large-scale under Good Laboratory Manufacturing Practice (GMP) conditions for therapeutic application in humans.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesCathelicidinsCloning, MolecularCost-Benefit AnalysisEscherichia coliImmunologic FactorsPeptidesRecombinant Fusion ProteinsAnti-Bacterial AgentsAnti-Infective AgentsAntimicrobial Cationic PeptidesCathelicidinsImmunologic FactorsPeptidesRecombinant Fusion Proteins

Identifiers

PMID20713107
PMCPMC2992949

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.