Project description:The archetypical venomous lizard species are the helodermatids, the Gila Monster (Heloderma suspectum) and the Beaded Lizards (Heloderma horridum). In the present study, the gila monster venom proteome was characterized using 2D-gel electrophoresis and tandem mass spectrometry-based de novo peptide sequencing followed by protein identification based on sequence homology. A total of 39 different proteins were identified out of the 58 selected spots that represent the major constituents of venom. Of these proteins, 19 have not previously been identified in helodermatid venom. The data showed that helodermatid venom is complex and that this complexity is caused by genetic isoforms and post-translational modifications including proteolytic processing. In addition, the venom proteome analysis revealed that the major constituents of the gila monster venom are kallikrein-like serine proteinases (EC 3.4.21) and phospholipase A2 (type III) enzymes (EC 3.1.1.4). A neuroendocrine convertase 1 homolog that most likely converts the proforms of the previously identified bioactive exendins into the mature and active forms was identified suggesting that these peptide toxins are secreted as proforms that are activated by proteolytic cleavage following secretion as opposed to being activated intracellularly. The presented global protein identification-analysis provides the first overview of the helodermatid venom composition.
Project description:The data presented here is related to the research article entitled "Characterization of the gila monster (Heloderma suspectum suspectum) venom proteome" by Sanggaard et al. in Journal of Proteomics [1]. The gila monster venom was collected, analyzed by 2D-gel electrophoresis and after Coomassie-Brilliant Blue staining the major spots were excised, subjected to in-gel trypsin digestion, and analyzed by LC-MS/MS. Subsequently, the venom proteins were identified based on de novo sequencing and homology searching. The mass spectrometry proteomics data have been deposited to the ProteomeXchange (dataset identifier PXD0001343), and in the present article we present an overview of the identified proteins. Protein identification failed for three of the selected spots, with the method described above. Instead, an iterative process, based on de novo sequencing, was employed.
Project description:The timing of reproductive events (e.g. oviposition and hatching) to coincide with favourable seasonal conditions is critical for successful reproduction. However, developmental time may not match the duration between the optimal time for oviposition and the optimal time for hatchling survival. Thus, strategies that alter the time between oviposition and hatchling emergence can be highly advantageous. Arrested development and the resulting extension of the duration between oviposition and hatching has been widely documented across oviparous amniotes, but nest overwintering by hatchlings has only been documented in aquatic chelonians that live where winters are quite cold. Herein, we present a compilation of evidence regarding reproductive phenology by hatchlings of the Gila monster (Heloderma suspectum), a lizard inhabiting the Sonoran Desert of North America. Our data demonstrate that (i) Gila monster hatchlings from eggs oviposited in July do not emerge from their nests until late spring or summer of the following year, yet (ii) Gila monster eggs artificially incubated at field-relevant temperatures hatch in 4-5 months. Furthermore, we describe a fortuitous excavation of a hatching Gila monster nest in late October, which coincides with the artificial incubation results. Together, these results provide strong support for the existence of overwintering in the nest by a lizard, and suggest that this reproductive strategy should be explored in a broader array of taxa.