Evidence map›Paper›PMID 30191288›Full record

ArticleApplied microbiology and biotechnology2018

Engineering recombinant Lactococcus lactis as a delivery vehicle for BPC-157 peptide with antioxidant activities.

Katja Škrlec, Rudolf Ručman, Eva Jarc, Predrag Sikirić, Urban Švajger, Toni Petan, Milica Perišić Nanut, Borut Štrukelj, Aleš Berlec

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
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 at 6 institutions in 2 countries.

Katja ŠkrlecDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Rudolf RučmanDiagen d.o.o, Šmartno, Ljubljana, Slovenia.
Eva JarcDepartment of Molecular and Biomedical Sciences, Jožef Stefan Institute, Ljubljana, Slovenia.
Predrag SikirićDepartment of Pharmacology and Pathology, Medical Faculty, University of Zagreb, Zagreb, Croatia.
Urban ŠvajgerBlood Transfusion Centre of Slovenia, Ljubljana, Slovenia.
Toni PetanDepartment of Molecular and Biomedical Sciences, Jožef Stefan Institute, Ljubljana, Slovenia.
Milica Perišić NanutDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Borut ŠtrukeljDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Aleš BerlecDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia. ales.berlec@ijs.si.
Jožef Stefan Institute · SIB2 (Slovenia) · SIBlood Transfusion Centre of Slovenia · SIJožef Stefan International Postgraduate School · SIUniversity of Ljubljana · SIUniversity of Zagreb · HR

Funding

Javna Agencija za Raziskovalno Dejavnost RS P4-0127
6 · The paper itself

Abstract

Lactic acid bacteria (LAB) are attractive hosts for the expression of heterologous proteins and can be engineered to deliver therapeutic proteins or peptides to mucosal surfaces. The gastric stable pentadecapeptide BPC-157 is able to prevent and treat gastrointestinal inflammation by reducing the production of reactive oxygen species (ROS). In this study, we used LAB Lactococcus lactis as a vector to deliver BPC-157 by surface display and trypsin shedding or by secretion to the growth medium. Surface display of BPC-157 was achieved by fusing it with basic membrane protein A (BmpA) or with the peptidoglycan binding domain of AcmA and Usp45 secretion signal. While the expression of BmpA-fusion proteins was higher than that of AcmA/Usp45-fusion protein, the surface display ability of BPC-157 was approximately 14-fold higher with AcmA/Usp45-fusion protein. Release of BPC-157 from the bacterial surface or from isolated fusion proteins by trypsinization was demonstrated with anti-BPC-157 antibodies or by mass spectrometry. The concentration of BPC-157 delivered by surface display via AcmA/Usp45-fusion was 30 ng/ml. This increased to 117 ng/ml by Usp45 signal-mediated secretion, making the latter the most effective lactococcal delivery approach for BPC-157. Secreted BPC-157 significantly decreased ROS production in 149BR fibroblast cell model, suggesting its potential benefit in the treatment of intestinal inflammations. Additionally, a comparison of different modes of small peptide delivery by L. lactis, performed in the present study, will facilitate the future use of L. lactis as peptide delivery vehicle.

Indexed as

Drug Delivery SystemsLactococcus lactisCell LineFibroblastsHumansInflammatory Bowel DiseasesMicroorganisms, Genetically-ModifiedOxidative StressPeptide FragmentsPlasmidsProtein EngineeringProteinsReactive Oxygen SpeciesRecombinant Fusion ProteinsBPC 157Peptide FragmentsProteinsReactive Oxygen SpeciesRecombinant Fusion ProteinsAntioxidantBPC-157FibroblastsLactococcus lactisPeptide deliveryRecombinant

Identifiers

PMID30191288
OpenAlexW2891575480

What OpenQuestion holds

Textmetadata
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.