| Autor: |
Estrada-Gomez S; Programa de Ofidismo/Escorpionismo-Serpentario, Universidad de Antioquia UdeA, Carrera 53 No 61-30, Medellín, Antioquia, CO 050010, Colombia. sebastian.estrada@udea.edu.co.; Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Calle 70 No 52-21, Medellín, Antioquia, CO 050010, Colombia. sebastian.estrada@udea.edu.co., Cardoso FC; Institute for Molecular Bioscience, The University of Queensland, 306 Carmody Road, St Lucia, QLD 4072, Australia., Vargas-Muñoz LJ; Facultad de Medicina, Universidad Cooperativa de Colombia, Calle 50 A No 41-20 Medellín, Antioquia, CO 050012, Colombia., Quintana-Castillo JC; Facultad de Medicina, Universidad Cooperativa de Colombia, Calle 50 A No 41-20 Medellín, Antioquia, CO 050012, Colombia., Arenas Gómez CM; Grupo de Génetica, Regeneración y Cáncer, Universidad de Antioquia UdeA, Carrera 53 No 61-30, Medellín, Antioquia, CO 050010, Colombia., Pineda SS; Brain and Mind Centre, University of Sydney, Camperdown, NSW 2052, Australia.; Garvan Institute of Medical Research, Darlinghurst, Sydney, NSW 2010, Australia.; St. Vincent's Clinical School, University of New South Wales, Sydney, NSW 2010, Australia., Saldarriaga-Cordoba MM; Centro de Investigación en Recursos Naturales y Sustentabilidad, Universidad Bernardo O'Higgins, Avenida Viel 1497, Santiago 7750000, Chile. |
| Abstrakt: |
Pamphobeteus verdolaga is a recently described Theraphosidae spider from the Andean region of Colombia. Previous reports partially characterized its venom profile. In this study, we conducted a detailed analysis that includes reversed-phase high-performance liquid chromatography (rp-HPLC), calcium influx assays, tandem mass spectrometry analysis (tMS/MS), and venom-gland transcriptome. rp-HPLC fractions of P. verdolaga venom showed activity on Ca V 2.2, Ca V 3.2, and Na V 1.7 ion channels. Active fractions contained several peptides with molecular masses ranging from 3399.4 to 3839.6 Da. The tMS/MS analysis of active fraction displaying the strongest activity to inhibit calcium channels showed sequence fragments similar to one of the translated transcripts detected in the venom-gland transcriptome. The putative peptide of this translated transcript corresponded to a toxin, here named ω-theraphositoxin-Pv3a, a potential ion channel modulator toxin that is, in addition, very similar to other theraphositoxins affecting calcium channels (i.e., ω-theraphotoxin-Asp1a). Additionally, using this holistic approach, we found that P. verdolaga venom is an important source of disulfide-rich proteins expressing at least eight superfamilies. |
