Comparative venomic profiles of three spiders of the genus Phoneutria

• Published in: The journal of venomous animals and toxins including tropical diseases Vol. 28; p. e20210042
• Main Authors: Fernandes, Frederico Francisco, Moraes, Juliana Rodrigues, Dos Santos, Jaqueline Leal, Soares, Thiago Geraldo, Gouveia, Vitor José Pinto, Matavel, Alessandra C S, Borges, William de Castro, Cordeiro, Marta do Nascimento, Figueiredo, Suely Gomes, Borges, Márcia Helena
• Format: Journal Article
• Language: English; Portuguese
• Published: Brazil Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP) 2022; SciELO
• Subjects: Ion channels; Phoneutria; Protein profile; Spider venom; TOXICOLOGY; Toxins; TROPICAL MEDICINE; Ion channels; Spider venom; Toxins; Phoneutria; Protein profile
• ISSN: 1678-9199; 1678-9199
• DOI: 10.1590/1678-9199-JVATITD-2021-0042

Spider venoms induce different physio-pharmacological effects by binding with high affinity on molecular targets, therefore being of biotechnological interest. Some of these toxins, acting on different types of ion channels, have been identified in the venom of spiders of the genus , mainly from . In spite of the pharmaceutical potential demonstrated by toxins, there is limited information on molecules from venoms of the same genus, as their toxins remain poorly characterized. Understanding this diversity and clarifying the differences in the mechanisms of action of spider toxins is of great importance for establishing their true biotechnological potential. This prompted us to compare three different venoms of the genus: (Pn-V), (Pe-V) and (Pp-V). Biochemical and functional comparison of the venoms were carried out by SDS-PAGE, HPLC, mass spectrometry, enzymatic activities and electrophysiological assays (whole-cell patch clamp). The employed approach revealed that all three venoms had an overall similarity in their components, with only minor differences. The presence of a high number of similar proteins was evident, particularly toxins in the mass range of ~6.0 kDa. Hyaluronidase and proteolytic activities were detected in all venoms, in addition to isoforms of the toxins Tx1 and Tx2-6. All Tx1 isoforms blocked Nav1.6 ion currents, with slight differences. Our findings showed that Pn-V, Pe-V and Pp-V are highly similar concerning protein composition and enzymatic activities, containing isoforms of the same toxins sharing high sequence homology, with minor modifications. However, these structural and functional variations are very important for venom diversity. In addition, our findings will contribute to the comprehension of the molecular diversity of the venoms of the other species from genus, exposing their biotechnological potential as a source for searching for new active molecules.