ArticleMolecular & cellular proteomics : MCP2016
Mapping Proteoforms and Protein Complexes From King Cobra Venom Using Both Denaturing and Native Top-down Proteomics.
Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 86 citations in OpenAlex.
- Article
- Molecular Mechanisms of Venom Diversity.Toxins · 2025Review
- Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions.International journal of molecular sciences · 2025Review
- Urinary proteomics reveals biological processes related to acute kidney injury in Bothrops atrox envenomings.PLoS neglected tropical diseases · 2024Article
- Mass Spectrometry Strategies forCells · 2024Review
- Article
- Multidimensional Separations in Top-Down Proteomics.Analytical science advances · 2023Article
- Venom characterization of the Brazilian Pampa snake Bothrops pubescens by top-down and bottom-up proteomics.Toxicon : official journal of the International Society on Toxinology · 2022Article
- Extracellular Vesicles fromToxins · 2022Article
- Modern venomics-Current insights, novel methods, and future perspectives in biological and applied animal venom research.GigaScience · 2022Article
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Endogenous Fluorescent Proteins in the Mucus of an Intertidal Polychaeta: Clues for Biotechnology.Marine drugs · 2022Article
- Surface-Induced Dissociation for Protein Complex Characterization.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Combined Molecular and Elemental Mass Spectrometry Approaches for Absolute Quantification of Proteomes: Application to the Venomics Characterization of the Two Species of Desert Black Cobras,Journal of proteome research · 2021Article
- Mass spectrometry-based top-down and bottom-up approaches for proteomic analysis of the Moroccan Buthus occitanus scorpion venom.FEBS open bio · 2021Article
- Article
- King Cobra and snakebite envenomation: on the natural history, human-snake relationship and medical importance ofThe journal of venomous animals and toxins including tropical diseases · 2021Review
- Integrating Top-Down and Bottom-Up Mass Spectrometric Strategies for Proteomic Profiling of Iranian Saw-Scaled Viper,Journal of proteome research · 2021Article
- Investigating Toxin Diversity and Abundance in Snake Venom Proteomes.Frontiers in pharmacology · 2021Review
- Proteomic Investigations of Two PakistaniToxins · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Characterizing whole proteins by top-down proteomics avoids a step of inference encountered in the dominant bottom-up methodology when peptides are assembled computationally into proteins for identification. The direct interrogation of whole proteins and protein complexes from the venom of Ophiophagus hannah (king cobra) provides a sharply clarified view of toxin sequence variation, transit peptide cleavage sites and post-translational modifications (PTMs) likely critical for venom lethality. A tube-gel format for electrophoresis (called GELFrEE) and solution isoelectric focusing were used for protein fractionation prior to LC-MS/MS analysis resulting in 131 protein identifications (18 more than bottom-up) and a total of 184 proteoforms characterized from 14 protein toxin families. Operating both GELFrEE and mass spectrometry to preserve non-covalent interactions generated detailed information about two of the largest venom glycoprotein complexes: the homodimeric l-amino acid oxidase (∼130 kDa) and the multichain toxin cobra venom factor (∼147 kDa). The l-amino acid oxidase complex exhibited two clusters of multiproteoform complexes corresponding to the presence of 5 or 6 N-glycans moieties, each consistent with a distribution of N-acetyl hexosamines. Employing top-down proteomics in both native and denaturing modes provides unprecedented characterization of venom proteoforms and their complexes. A precise molecular inventory of venom proteins will propel the study of snake toxin variation and the targeted development of new antivenoms or other biotherapeutics.
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