Evidence map›Paper›PMID 32483218›Full record

ArticleScientific reports2020

Environmental and dynamic effects explain how nisin captures membrane-bound lipid II.

Irina Panina, Nikolay Krylov, Dmitry Nolde, Roman Efremov, Anton Chugunov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. 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
1.9field-weighted citation impact, top 14% 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, 36 citations in OpenAlex.

  1. Review
  2. Review
  3. Lactic Acid Bacteria Bacteriocins: Safe and Effective Antimicrobial Agents.International journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Nisin S, a Novel Nisin Variant Produced byInternational journal of molecular sciences · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
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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

5 authors at 1 institution in 1 country.

Irina PaninaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya St., Moscow, 117997, Russia.ORCID http://orcid.org/0000-0003-0379-3782
Nikolay KrylovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya St., Moscow, 117997, Russia.
Dmitry NoldeShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya St., Moscow, 117997, Russia.ORCID http://orcid.org/0000-0002-3328-0024
Roman Efremov *Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya St., Moscow, 117997, Russia. r-efremov@yandex.ru.
Anton Chugunov *Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya St., Moscow, 117997, Russia.ORCID http://orcid.org/0000-0003-1331-3949
National Research University Higher School of Economics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibiotics (AB) resistance is a major threat to global health, thus the development of novel AB classes is urgently needed. Lantibiotics (i.e. nisin) are natural compounds that effectively control bacterial populations, yet their clinical potential is very limited. Nisin targets membrane-embedded cell wall precursor - lipid II - via capturing its pyrophosphate group (PPi), which is unlikely to evolve, and thus represents a promising pharmaceutical target. Understanding of exact molecular mechanism of initial stages of membrane-bound lipid II recognition by water-soluble nisin is indispensable. Here, using molecular simulations, we demonstrate that the structure of lipid II is determined to a large extent by the surrounding water-lipid milieu. In contrast to the bulk solvent, in the bilayer only two conformational states remain capable of nisin binding. In these states PPi manifests a unique arrangement of hydrogen bond acceptors on the bilayer surface. Such a "pyrophosphate pharmacophore" cannot be formed by phospholipids, which explains high selectivity of nisin/lipid II recognition. Similarly, the "recognition module" of nisin, being rather flexible in water, adopts the only stable conformation in the presence of PPi analogue (which mimics the lipid II molecule). We establish the "energy of the pyrophosphate pharmacophore" approach, which effectively distinguishes nisin conformations that can form a complex with PPi. Finally, we propose a molecular model of nisin recognition module/lipid II complex in the bacterial membrane. These results will be employed for further study of lipid II targeting by antimicrobial (poly)cyclic peptides and for design of novel AB prototypes.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsComputational ChemistryDimethyl SulfoxideDiphosphatesHydrogen BondingLipid BilayersMembrane LipidsModels, ChemicalModels, MolecularMolecular ConformationNisinNuclear Magnetic Resonance, BiomolecularPhosphatidylethanolaminesPhosphatidylglycerolsProtein Binding1-palmitoyl-2-oleoylglycero-3-phosphoglycerol1-palmitoyl-2-oleoylphosphatidylethanolamineAnti-Bacterial AgentsDimethyl SulfoxideDiphosphatesdiphosphoric acidLipid BilayersMembrane Lipidsmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolNisinPhosphatidylethanolaminesPhosphatidylglycerolsUridine Diphosphate N-Acetylmuramic AcidWater

Identifiers

PMID32483218
PMCPMC7264305
OpenAlexW3032471731

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Registered trials

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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.