The Potassium Channel Blocker β-Bungarotoxin from the Krait <i>Bungarus multicinctus</i> Venom Manifests Antiprotozoal Activity
2023
Alexey V. Osipov | Elena G. Cheremnykh | Rustam H. Ziganshin | Vladislav G. Starkov | Trang Thuy Thi Nguyen | Khoa Cuu Nguyen | Dung Tien Le | Anh Ngoc Hoang | Victor I. Tsetlin | Yuri N. Utkin
Protozoal infections are a world-wide problem. The toxicity and somewhat low effectiveness of the existing drugs require the search for new ways of protozoa suppression. Snake venom contains structurally diverse components manifesting antiprotozoal activity; for example, those in cobra venom are cytotoxins. In this work, we aimed to characterize a novel antiprotozoal component(s) in the <i>Bungarus multicinctus</i> krait venom using the ciliate <i>Tetrahymena pyriformis</i> as a model organism. To determine the toxicity of the substances under study, surviving ciliates were registered automatically by an original BioLaT-3.2 instrument. The krait venom was separated by three-step liquid chromatography and the toxicity of the obtained fractions against <i>T. pyriformis</i> was analyzed. As a result, 21 kDa protein toxic to <i>Tetrahymena</i> was isolated and its amino acid sequence was determined by MALDI TOF MS and high-resolution mass spectrometry. It was found that antiprotozoal activity was manifested by β-bungarotoxin (β-Bgt) differing from the known toxins by two amino acid residues. Inactivation of β-Bgt phospholipolytic activity with <i>p</i>-bromophenacyl bromide did not change its antiprotozoal activity. Thus, this is the first demonstration of the antiprotozoal activity of β-Bgt, which is shown to be independent of its phospholipolytic activity.
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