Venom Mass Fingerprints for Species Delimitation, Reloaded: A Test Case with Italian Scorpions (Euscorpius)

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  Venom Mass Fingerprints for Species Delimitation, Reloaded: A Test Case with Italian Scorpions (Euscorpius) Abstract Scorpion venoms are complex mixtures of bioactive compounds including proteins, peptides and enzymes. Although venoms exhibit substantial intraspecific variation, some compounds appear to be species-specific, highlighting their potential as chemotaxonomic markers. Venom mass fingerprints (MFPs) derived from Matrix-Assisted Laser Desorption/Ionization Time-of-Flight (MALDI-TOF) Mass Spectrometry (MS) have been proposed as a means of delimiting species. However, their utility for species delimitation has rarely been evaluated against independent sources of taxonomic evidence. In the present study, the performance of MALDI-TOF MS-based venom peptide barcoding (mass ranges of m/z 800‒4500 and m/z 3000‒10,000) was assessed in 52 populations of eight Italian species of the scorpion genus Euscorpius Thorell, 1876, representing different levels of evolutionary divergenc...

Broad-Spectrum Antiviral and Antibacterial Activity of the Scorpion Venom Peptide HP1090

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Broad-Spectrum Antiviral and Antibacterial Activity of the Scorpion Venom Peptide HP1090

Abstract

HP1090 is a short, cationic, amphipathic peptide derived from scorpion venom and previously described as a membrane-active antiviral compound. Here, we primarily characterize the antiviral activity of HP1090 and assess whether additional antibacterial effects are consistent with membrane-disruptive properties. Chemically synthesized HP1090 exhibited dose-dependent virucidal activity against multiple enveloped viruses, including herpes simplex virus type 1 and 2 (HSV-1, HSV-2), human immunodeficiency virus type 1 (HIV-1), and Zika virus (ZIKV), with IC50 values ranging from 14.7 to 56.1 µg/mL. No activity was observed against the non-enveloped human rhinovirus 14 (HRV14), suggesting strict dependence on a viral lipid envelope. Consistent with a membrane-targeting mechanism, HP1090 induced rapid and concentration-dependent permeabilization of virus-like liposomes. HP1090 also displayed antibacterial activity against selected clinically relevant pathogens in agar-based growth inhibition assays. However, antibacterial effects required substantially higher concentrations (>125 µg/mL) and varied between bacterial species, with some strains showing little or no susceptibility. Membrane permeabilization assays in Listeria monocytogenes demonstrated disruption of bacterial membrane integrity as a contributing mechanism. No cytotoxicity was observed on mammalian cell lines at effective antiviral concentrations. Together, these findings establish HP1090 as a membrane-active venom peptide and, by linking envelope-dependent viral inactivation with bacterial membrane permeabilization, support a shared biophysical mode of action relevant to the development of membrane-targeting anti-infectives.

Asuzano, A. J., Olari, L. R., Jaber, N., Vogel, V., Fam, M. S., Rodríguez Alfonso, A. A., Preising, N., Ständker, L., Spellerberg, B., Breitinger, H. G., Breitinger, U., & Münch, J. (2026). Broad-Spectrum Antiviral and Antibacterial Activity of the Scorpion Venom Peptide HP1090. Toxins. https://doi.org/10.3390/toxins18060268