Rattlesnake's venom constitutes an important ecological trait that dynamically changes over time. Venoms of adult and juvenile rattleless rattlesnakes, Crotalus catalinensis, an endemic insular species from the Gulf of California, were compared by electrophoretic profile, fibrinogenolytic activity, and proteomic composition to assess ontogenetic variability. The SDS-PAGE profiles show important differences at 12, 22, and 45 kDa, which were prominent in adult samples and absent in juvenile samples, while bands around 20, 25, and 70 kDa are almost absent in adults. Both venoms hydrolyze Aa and Bb chains of fibrinogen generating different patterns of degradation products. This activity was partially inhibited by EDTA and PMSF and completely abolished only in the presence of both inhibitors. More than 260 proteins were identified and quantified in both venoms by proteomic analysis. Metalloproteinases (more than 60%), serine proteinases (14.5% in adult venom and 17.7% in juvenile venom), and C-type lectins (7.1 and 5.9%) represent the three most abundant toxin-related protein families. Bradykinin inhibitor peptides and L-amino acid oxidases were not detected in juvenile venom. A protein-specific comparison shows that adult and juvenile venom share about 30.5% of total toxin-related proteins, while 32% and 35% are exclusively present in adult and juvenile venoms, respectively. This work represents one of the first efforts to understand phenotypic diversity in the venom composition of insular rattlesnake species from Mexico.
Keywords: Crotalus catalinensis; Mass spectrometry; Ontogenetic variation; Toxin; Venom composition; Venomics.
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