Evidence map›Paper›PMID 33574430›Full record

ArticleScientific reports2021

Identification, heterologous production and bioactivity of lentinulin A and dendrothelin A, two natural variants of backbone N-methylated peptide macrocycle omphalotin A.

Emmanuel Matabaro, Hannelore Kaspar, Paul Dahlin, Daniel L V Bader, Claudia E Murar, Florian Staubli, Christopher M Field, Jeffrey W Bode, Markus Künzler

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 27 citations in OpenAlex.

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  12. Diverse Protein Architectures and α-ACS chemical biology · 2022
    Article
  13. Engineering of a Peptide α-N-Methyltransferase to Methylate Non-Proteinogenic Amino Acids.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Emmanuel MatabaroDepartment of Biology, Institute of Microbiology, ETH Zürich, Room HCI F409, Vladimir-Prelog-Weg 4, CH-8093, Zürich, Switzerland.
Hannelore KasparDepartment of Biology, Institute of Microbiology, ETH Zürich, Room HCI F409, Vladimir-Prelog-Weg 4, CH-8093, Zürich, Switzerland.
Paul DahlinAgroscope, Phytopathology and Zoology in Fruit and Vegetable Production, Müller-Thurgau-Strasse 29, CH-8820, Wädenswil, Switzerland.ORCID http://orcid.org/0000-0002-9945-8059
Daniel L V BaderDepartment of Chemistry and Applied Biosciences, Laboratorium Für Organische Chemie, ETH-Zürich, Vladimir-Prelog-Weg 3, CH-8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-7731-0494
Claudia E MurarDepartment of Chemistry and Applied Biosciences, Laboratorium Für Organische Chemie, ETH-Zürich, Vladimir-Prelog-Weg 3, CH-8093, Zürich, Switzerland.
Florian StaubliDepartment of Biology, Institute of Microbiology, ETH Zürich, Room HCI F409, Vladimir-Prelog-Weg 4, CH-8093, Zürich, Switzerland.
Christopher M FieldDepartment of Biology, Institute of Microbiology, ETH Zürich, Room HCI F409, Vladimir-Prelog-Weg 4, CH-8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-6434-3745
Jeffrey W BodeDepartment of Chemistry and Applied Biosciences, Laboratorium Für Organische Chemie, ETH-Zürich, Vladimir-Prelog-Weg 3, CH-8093, Zürich, Switzerland.ORCID http://orcid.org/0000-0001-8394-8910
Markus KünzlerDepartment of Biology, Institute of Microbiology, ETH Zürich, Room HCI F409, Vladimir-Prelog-Weg 4, CH-8093, Zürich, Switzerland. mkuenzle@ethz.ch.ORCID https://orcid.org/0000-0003-1275-0629
ETH Zurich · CHAgroscope · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Backbone N-methylation and macrocyclization improve the pharmacological properties of peptides by enhancing their proteolytic stability, membrane permeability and target selectivity. Borosins are backbone N-methylated peptide macrocycles derived from a precursor protein which contains a peptide α-N-methyltransferase domain autocatalytically modifying the core peptide located at its C-terminus. Founding members of borosins are the omphalotins from the mushroom Omphalotus olearius (omphalotins A-I) with nine out of 12 L-amino acids being backbone N-methylated. The omphalotin biosynthetic gene cluster codes for the precursor protein OphMA, the protease prolyloligopeptidase OphP and other proteins that are likely to be involved in other post-translational modifications of the peptide. Mining of available fungal genome sequences revealed the existence of highly homologous gene clusters in the basidiomycetes Lentinula edodes and Dendrothele bispora. The respective borosins, referred to as lentinulins and dendrothelins are naturally produced by L. edodes and D. bispora as shown by analysis of respective mycelial extracts. We produced all three homologous peptide natural products by coexpression of OphMA hybrid proteins and OphP in the yeast Pichia pastoris. The recombinant peptides differ in their nematotoxic activity against the plant pathogen Meloidogyne incognita. Our findings pave the way for the production of borosin peptide natural products and their potential application as novel biopharmaceuticals and biopesticides.

Indexed as

AgaricalesAnimalsGene Expression Regulation, FungalGenome, FungalMethylationMethyltransferasesPeptide HydrolasesPeptidesPeptides, CyclicProteolysisSaccharomycetalesShiitake MushroomsTylenchoideaMethyltransferasesoligopeptidaseomphalotin APeptide HydrolasesPeptidesPeptides, Cyclic

Identifiers

PMID33574430
PMCPMC7878506
OpenAlexW3126332741

What OpenQuestion holds

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LicenceCC BY
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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.