Dataset Information

Proteomic analysis of Heloderma horridum horridum venom

ABSTRACT: 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.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Heloderma Horridum Horridum

TISSUE(S): Protein Secretion, Venom

SUBMITTER: Miguel Elizalde

LAB HEAD: Eliel Ruiz-May

PROVIDER: PXD052417 | Pride | 2024-08-10

REPOSITORIES: pride

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Proteomic Analysis of Heloderma horridum horridum Venom: Assessment to Its Transcriptome and Newfound Proteins.

Lino-López Gisela J GJ Ruiz-May Eliel E Elizalde-Contreras José M JM Jiménez-Vargas Juana M JM Rodríguez-Vázquez Armando A González-Carrillo Gabino G Bojórquez-Velázquez Esaú E García-Villalvazo Patricia E PE Bermúdez-Guzmán Manuel de J MJ Zatarain-Palacios Rocio R Vázquez-Vuelvas Oscar F OF Valdez-Velázquez Laura L LL Corzo Gerardo G

Journal of proteome research 20240722 8

Heloderma horridum horridum, a venomous reptile native to America, has a venom with potential applications in treating type II diabetes. In this work, H. h. horridum venom was extracted, lyophilized, and characterized using enzymatic assays for hyaluronidase, phospholipase, and protease. Proteomic analysis of the venom was conducted employing bottom-up/shotgun approaches, SDS-PAGE, high-pH reversed-phase chromatography, and fractionation of tryptic peptides using nano-LC-MS/ ...[more]

PMID: 39038168

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Project description:Spider venoms are a unique source of bioactive peptides displaying remarkable structural stability and potent neuroactivity. Phoneutria nigriventer, often referred to as Brazilian wandering spider, banana spider or “armed” spider, is endemic from South America and amongst the most dangerous venomous spiders in the world. Envenomation accidents with P. nigriventer often occur in Brazil with approximately 4,000 cases per year and which symptoms include priapism, hypertension, blurred vision, sweating, and vomiting, amongst others. Besides its clinical relevance, P. nigriventer venom comprises promising peptide drug leads providing therapeutic effects in a range of disease models. In this study, we further explored the neuroactivity and molecular diversity of the venom from P. nigriventer using fractionation-guided high-throughput cellular assays coupled to proteomics analysis and multi-pharmacology activity to broaden the knowledge and therapeutic potential of this venom, as well as a proof-of-concept for an investigative pipeline to study spider-venom derived neuroactive peptides. We applied ion channel assays in a neuroblastoma cell line to investigate modulation of voltage-gated sodium and calcium channels, and nicotinic acetylcholine α7 receptor. We then investigated the venom components using mass spectrometry to identify peptide masses and sequences associated to the observed neuromodulations. Our findings showed this venom is highly complex compared to other neurotoxin-rich venoms and comprises potent modulators of voltage-gated sodium and calcium channels which were classified into 4 families of neuroactive peptides based on their activities and structures. In addition to the reported P. nigriventer neuroactive peptides, we identified at least 27 novel cysteine-rich venom peptides in which neuroactivities are still to be elucidated in voltage-gated ion channels and other potential targets. Our findings provide a new basis for studying non-explored bioactivities of known and novel neuroactive components in P. nigriventer venom, and further supports the successful application of our discovery pipeline for identifying ion channel-targeting venom peptides with potential to become drug leads with diverse exploratory and therapeutic applications.

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Dataset Information

Proteomic analysis of Heloderma horridum horridum venom

Dataset's files

Publications

Proteomic Analysis of <i>Heloderma horridum horridum</i> Venom: Assessment to Its Transcriptome and Newfound Proteins.

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