Evidence map›Paper›PMID 27443638›Full record

ArticleScientific reports2016

The first non Clostridial botulinum-like toxin cleaves VAMP within the juxtamembrane domain.

Irene Zornetta, Domenico Azarnia Tehran, Giorgio Arrigoni, Fabrizio Anniballi, Luca Bano, Oneda Leka, Giuseppe Zanotti, Thomas Binz, Cesare Montecucco

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed, 1 pooled it
10.8field-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

65 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.

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5 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 at 4 institutions in 2 countries.

Irene ZornettaDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, Padova, Italy.
Domenico Azarnia TehranDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, Padova, Italy.
Giorgio ArrigoniDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, Padova, Italy.
Fabrizio AnniballiNational Reference Center for Botulism, Department of Veterinary Public Health and Food Safety, Istituto Superiore di Sanità (ISS), Roma, Italy.
Luca BanoMicrobiology and Diagnostic Laboratory, Istituto Zooprofilattico Sperimentale delle Venezie (IZSVe), Vicolo Mazzini 4, Villorba di Treviso, Italy.
Oneda LekaDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, Padova, Italy.
Giuseppe ZanottiDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, Padova, Italy.
Thomas BinzMedizinische Hochschule Hannover, Institut für Physiologische Chemie OE4310, Hannover, Germany.
Cesare MontecuccoDepartment of Biomedical Sciences, University of Padova, Via Ugo Bassi 58/B, Padova, Italy.
University of Padua · ITIstituto Superiore di Sanità · ITIstituto Zooprofilattico Sperimentale delle Venezie · ITMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genome of Weissella oryzae SG25T was recently sequenced and a botulinum neurotoxin (BoNT) like gene was identified by bioinformatics methods. The typical three-domains organization of BoNTs with a N-terminal metalloprotease domain, a translocation and a cell binding domains could be identified. The BoNT family of neurotoxins is rapidly growing, but this was the first indication of the possible expression of a BoNT toxin outside the Clostridium genus. We performed molecular modeling and dynamics simulations showing that the 50 kDa N-terminal domain folds very similarly to the metalloprotease domain of BoNT/B, whilst the binding part is different. However, neither the recombinant metalloprotease nor the binding domains showed cross-reactivity with the standard antisera that define the seven serotypes of BoNTs. We found that the purified Weissella metalloprotease cleaves VAMP at a single site untouched by the other VAMP-specific BoNTs. This site is a unique Trp-Trp peptide bond located within the juxtamembrane segment of VAMP which is essential for neurotransmitter release. Therefore, the present study identifies the first non-Clostridial BoNT-like metalloprotease that cleaves VAMP at a novel and relevant site and we propose to label it BoNT/Wo.

Indexed as

Amino Acid SequenceBotulinum ToxinsCell MembraneClostridium botulinumGenome, BacterialMetalloproteasesModels, MolecularMolecular Dynamics SimulationNeurotoxinsProtein BindingProtein DomainsProtein FoldingWeissellaBotulinum ToxinsMetalloproteasesNeurotoxins

Identifiers

PMID27443638
PMCPMC4957215
OpenAlexW2505402977

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.