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

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: 10.1371/journal.pone.0222206


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


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