Evidence map›Paper›PMID 33715301›Full record

ArticleFEBS open bio2021

Mass spectrometry-based top-down and bottom-up approaches for proteomic analysis of the Moroccan Buthus occitanus scorpion venom.

Khadija Daoudi, Christian Malosse, Ayoub Lafnoune, Bouchra Darkaoui, Salma Chakir, Jean-Marc Sabatier, Julia Chamot-Rooke, Rachida Cadi, Naoual Oukkache

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

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  11. Toxinology in the proteomics era: a review on arachnid venom proteomics.The journal of venomous animals and toxins including tropical diseases · 2022
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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

9 authors at 4 institutions in 4 countries.

Khadija DaoudiLaboratory of Venoms and Toxins, Pasteur Institute of Morocco, Casablanca, Morocco.ORCID 0000-0002-3079-1697
Christian MalosseMass spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, Paris, France.
Ayoub LafnouneLaboratory of Venoms and Toxins, Pasteur Institute of Morocco, Casablanca, Morocco.
Bouchra DarkaouiLaboratory of Venoms and Toxins, Pasteur Institute of Morocco, Casablanca, Morocco.
Salma ChakirLaboratory of Venoms and Toxins, Pasteur Institute of Morocco, Casablanca, Morocco.
Jean-Marc SabatierLaboratory INSERM UMR 1097, University of Aix Marseille, France.
Julia Chamot-RookeMass spectrometry for Biology Unit, Institut Pasteur, CNRS USR 2000, Paris, France.
Rachida CadiLaboratory of Molecular Genetics, Physiopathology and Biotechnology, Faculty of Sciences Ain Chock, Hassan II University of Casablanca, Morocco.
Naoual OukkacheLaboratory of Venoms and Toxins, Pasteur Institute of Morocco, Casablanca, Morocco.
Casablanca (Brazil) · BRCentre National de la Recherche Scientifique · FRInserm · FRUniversity of Hassan II Casablanca · MA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Buthus occitanus (B. occitanus) is one of the most dangerous scorpions in the world. Despite the involvement of B. occitanus scorpion in severe cases of envenomation in Morocco, no study has focused yet on the proteomic composition of the Moroccan B. occitanus scorpion venom. Mass spectrometry-based proteomic techniques are commonly used in the study of scorpion venoms. The implementation of top-down and bottom-up approaches for proteomic analyses facilitates screening by allowing a global view of the structural aspects of such complex matrices. Here, we provide a partial overview of the venom of B. occitanus scorpion, in order to explore the diversity of its toxins and hereafter understand their effects. To this end, a combination of top-down and bottom-up approaches was applied using nano-high liquid chromatography coupled to nano-electrospray tandem mass spectrometry (nano-LC-ESI MS/MS). The LC-MS results showed that B. occitanus venom contains around 200 molecular masses ranging from 1868 to 16 720 Da, the most representative of which are those between 5000 and 8000 Da. Interestingly, combined top-down and bottom-up LC-MS/MS results allowed the identification of several toxins, which were mainly those acting on ion channels, including those targeting sodium (NaScTxs), potassium (KScTxs), chloride (ClScTxs), and calcium channels (CaScTx), as well as antimicrobial peptides (AMPs), amphipathic peptides, myotropic neuropeptides, and hypothetical secreted proteins. This study reveals the molecular diversity of B. occitanus scorpion venom and identifies components that may have useful pharmacological activities.

Indexed as

ScorpionsScorpion VenomsAnimalsChromatography, LiquidProteomicsTandem Mass SpectrometryScorpion Venomsbottom-upButhus occitanus scorpiontop-downtoxinsvenomvenomic

Identifiers

PMID33715301
PMCPMC8255848
OpenAlexW3138999655

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.