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Comparative Proteomic Analysis of the Venoms from the Most Dangerous Scorpions in Morocco: Androctonus mauritanicus and Buthus occitanus - PubMed Skip to main page content
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. 2023 May 5;13(5):1133.
doi: 10.3390/life13051133.

Comparative Proteomic Analysis of the Venoms from the Most Dangerous Scorpions in Morocco: Androctonus mauritanicus and Buthus occitanus

Ines Hilal  1   2 , Soukaina Khourcha  1   2 , Amal Safi  2 , Abdelaziz Hmyene  2 , Syafiq Asnawi  3 , Iekhsan Othman  3 , Reto Stöcklin  4 , Naoual Oukkache  1
Affiliations

Comparative Proteomic Analysis of the Venoms from the Most Dangerous Scorpions in Morocco: Androctonus mauritanicus and Buthus occitanus

Ines Hilal et al. Life (Basel). .

Abstract

Morocco is known to harbor two of the world's most dangerous scorpion species: the black Androctonus mauritanicus (Am) and the yellow Buthus occitanus (Bo), responsible for 83% and 14% of severe envenomation cases, respectively. Scorpion venom is a mixture of biological molecules of variable structures and activities, most of which are proteins of low molecular weights referred to as toxins. In addition to toxins, scorpion venoms also contain biogenic amines, polyamines, and enzymes. With the aim of investigating the composition of the Am and Bo venoms, we conducted an analysis of the venoms by mass spectrometry (ESI-MS) after separation by reversed-phase HPLC chromatography. Results from a total of 19 fractions obtained for the Am venom versus 22 fractions for the Bo venom allowed the identification of approximately 410 and 252 molecular masses, respectively. In both venoms, the most abundant toxins were found to range between 2-5 kDa and 6-8 kDa. This proteomic analysis not only allowed the drawing of an extensive mass fingerprint of the Androctonus mauritanicus and Buthus occitanus venoms but also provided a better insight into the nature of their toxins.

Keywords: Androctonus mauritanicus; Buthus occitanus; mass fingerprinting; mass spectrometry; proteomics; scorpion; venom.

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Conflict of interest statement

The authors declared no potential conflict of interest with respect to the research, authorship, and/or publication of this article.

Figures

Figure 1
Figure 1
Electrophoretic profile of venoms on polyacrylamide gel in the presence of SDS in reducing conditions. Lane 1: molecular mass markers, Lane 2: Am venom, Lane 3: Bo venom.
Figure 2
Figure 2
Reversed-phase HPLC profile of 1 mg protein of Am and Bo venoms performed with a linear gradient from solvent A (0.1% TFA in water) to 100% solvent B (0.10% TFA in acetonitrile) at a flow rate of 1 mL/min over 120 min.
Figure 3
Figure 3
Total ion current chromatograms generated by LC-MS analysis of Am and Bo venoms.
Figure 4
Figure 4
Molecular mass distribution of Am and Bo Venoms.
Figure 5
Figure 5
Am and Bo venoms components.
Figure 6
Figure 6
Percentage of toxins in Am and Bo venoms.
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