Heloderma suspectum cinctum
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ABSTRACT:
PROVIDER: PRJNA189581 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Heloderma suspectum Genome sequencing and assembly
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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.
2015-01-26 | PXD001343 | Pride
Project description:Heloderma horridum horridum commonly known as the scorpion lizard, Mexican scorpion, and beaded lizard, is a venomous reptile native of America. The venom derived from this lizard has potential applications, particularly in treatment of type II diabetes through the peptide Exendin. In this work, H. h. horridum venom was extracted from adult specimens and lyophilized. To characterize the venom, enzymatic assays, including hyaluronidase, phospholipase A2, and proteolytic activity were conducted. A proteomic analysis of the venom was also performed employing bottom-up/shotgun approaches from SDS-PAGE and High pH Reversed-Phase chromatography., besides fractionation of tryptic peptides using a nano-LC-MS/MS. These approaches involved massive sequencing to enhancing the likelihood of detecting an extensive range of venom proteins. The proteins and peptides found in H. h. horridum venom are reviewed according to the classification of the transcriptome previously reported.
2024-08-10 | PXD052417 | Pride
Project description:Venom gland transcriptome analysis of the lizard Heloderma horridum horridum by RNA-Seq
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Project description:Interventions: A group:Before using cetuximab;B group:After progression of disease:no
Primary outcome(s): KRAS gene sequence;NRAS gene sequence;BRAF gene sequence;PIK3CA gene sequence;EGFR gene sequence;EGFR gene copy numbers;EGFR expression;Her2 expression;c-Met expression;PTEN expression
Study Design: historical control
| 2671639 | ecrin-mdr-crc
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.
| S-EPMC4510068 | biostudies-literature