Comparative compositional and functional analyses of Bothrops moojeni specimens reveal several individual variations

English version

Autoři: Weslei da Silva Aguiar ^aff001; Nathália da Costa Galizio ^aff001; Caroline Serino-Silva ^aff001; Sávio Stefanini Sant’Anna ^aff001; Kathleen Fernandes Grego ^aff001; Alexandre Keiji Tashima ^aff003; Erika Sayuri Nishiduka ^aff003; Karen de Morais-Zani ^aff001; Anita Mitico Tanaka-Azevedo ^aff001
Působiště autorů: Laboratório de Herpetologia, Instituto Butantan, São Paulo, Brasil ^aff001; Interunidades em Biotecnologia, Universidade de São Paulo, Instituto de Pesquisas Tecnológicas, Instituto Butantan, São Paulo, Brasil ^aff002; Departamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, Brasil ^aff003
Vyšlo v časopise: PLoS ONE 14(9)
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pone.0222206

Souhrn

Snake venoms are complex protein mixtures with different biological activities that can act in both their preys and human victims. Many of these proteins play a role in prey capture and in the digestive process of these animals. It is known that some snakes are resistant to the toxicity of their own venom by mechanisms not yet fully elucidated. However, it was observed in the Laboratory of Herpetology of Instituto Butantan that some Bothrops moojeni individuals injured by the same snake species showed mortalities caused by envenoming effects. This study analyzed the biochemical composition of 13 venom and plasma samples from Bothrops moojeni specimens to assess differences in their protein composition. Application of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed distinct venom protein profiles, but very homogeneous plasma profiles. Western Blotting (WB) was performed with plasma samples, which were submitted to incubation with the respective venom. Some individuals showed an immunorecognized band zone around 25 kDa, indicating interaction between the same individual plasma and venom proteins. Crossed-WB assay using non-self-plasma and venom showed that this variability is due to venom protein composition instead of plasma composition. These venoms presented higher caseinolytic, collagenolytic and coagulant activities than the venoms without these regions recognized by WB. Mass spectrometry analyses performed on two individuals revealed that these individuals present, in addition to higher protein concentrations, other exclusive proteins in their composition. When these same two samples were tested in vivo, the results also showed higher lethality in these venoms, but lower hemorrhagic activity than in the venoms without these regions recognized by WB. In conclusion, some Bothrops moojeni specimens differ in venom composition, which may have implications in envenomation. Moreover, the high individual venom variability found in this species demonstrates the importance to work with individual analyses in studies involving intraspecific venom variability and venom evolution.

Klíčová slova:

Biology and life sciences – Biochemistry – Organisms – Eukaryota – Enzymology – Enzymes – Proteins – Animals – Anatomy – Medicine and health sciences – Pathology and laboratory medicine – Physiology – Vertebrates – Amniotes – Diagnostic medicine – Signs and symptoms – Tropical diseases – Body fluids – Blood – Blood plasma – Vascular medicine – Reptiles – Squamates – Snakes – Neglected tropical diseases – Proteases – Toxicology – Toxic agents – Toxins – Hemorrhage – Plasma proteins – Venoms – Serine proteases – Snakebite

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Comparative compositional and functional analyses of Bothrops moojeni specimens reveal several individual variations

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