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- Title
The Potassium Channel Blocker β-Bungarotoxin from the Krait Bungarus multicinctus Venom Manifests Antiprotozoal Activity.
- Authors
Osipov, Alexey V.; Cheremnykh, Elena G.; Ziganshin, Rustam H.; Starkov, Vladislav G.; Nguyen, Trang Thuy Thi; Nguyen, Khoa Cuu; Le, Dung Tien; Hoang, Anh Ngoc; Tsetlin, Victor I.; Utkin, Yuri N.
- Abstract
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 Bungarus multicinctus krait venom using the ciliate Tetrahymena pyriformis 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 T. pyriformis was analyzed. As a result, 21 kDa protein toxic to Tetrahymena 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 p-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.
- Subjects
POTASSIUM antagonists; VENOM; SNAKE venom; AMINO acid residues; AMINO acid sequence
- Publication
Biomedicines, 2023, Vol 11, Issue 4, p1115
- ISSN
2227-9059
- Publication type
Article
- DOI
10.3390/biomedicines11041115