Evidence map›Paper›PMID 25854672›Full record

ArticleScientific reports2015

Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].

Marjetka Podobnik, Marta Marchioretto, Manuela Zanetti, Andrej Bavdek, Matic Kisovec, Miša Mojca Cajnko, Lorenzo Lunelli, Mauro Dalla Serra, Gregor Anderluh

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. 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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

39 citing papers in PubMed, 75 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 4 countries.

Marjetka PodobnikLaboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Marta MarchiorettoIstituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
Manuela ZanettiIstituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
Andrej BavdekDepartment of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
Matic KisovecLaboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Miša Mojca CajnkoLaboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Lorenzo LunelliIstituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
Mauro Dalla SerraIstituto di Biofisica, Consiglio Nazionale delle Ricerche &Fondazione Bruno Kessler, via alla Cascata 56/C, 38123 Trento, Italy.
Gregor Anderluh1] Laboratory for Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia [2] Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia.
Fondazione Bruno Kessler · ITNational Institute of Chemistry · SIUniversity of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pore formation of cellular membranes is an ancient mechanism of bacterial pathogenesis that allows efficient damaging of target cells. Several mechanisms have been described, however, relatively little is known about the assembly and properties of pores. Listeriolysin O (LLO) is a pH-regulated cholesterol-dependent cytolysin from the intracellular pathogen Listeria monocytogenes, which forms transmembrane β-barrel pores. Here we report that the assembly of LLO pores is rapid and efficient irrespective of pH. While pore diameters at the membrane surface are comparable at either pH 5.5 or 7.4, the distribution of pore conductances is significantly pH-dependent. This is directed by the unique residue H311, which is also important for the conformational stability of the LLO monomer and the rate of pore formation. The functional pores exhibit variations in height profiles and can reconfigure significantly by merging to other full pores or arcs. Our results indicate significant plasticity of large β-barrel pores, controlled by environmental cues like pH.

Indexed as

Hydrogen-Ion ConcentrationAmino Acid SequenceBacterial ToxinsCell MembraneHeat-Shock ProteinsHemolysin ProteinsHistidineListeria monocytogenesModels, MolecularMolecular Sequence DataMutationProtein AggregatesProtein ConformationProtein MultimerizationProtein StabilitySequence AlignmentBacterial ToxinsHeat-Shock ProteinsHemolysin ProteinsHistidinehlyA protein, Listeria monocytogenesProtein Aggregates

Identifiers

PMID25854672
PMCPMC5381700
OpenAlexW2011865356

What OpenQuestion holds

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LicenceCC BY
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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.