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. 2025 Jul 2;13(3):31.
doi: 10.3390/proteomes13030031.

Comparative Label-Based Proteomics of Venoms from Echis ocellatus, Naja nigricollis, and Bitis arietans

Affiliations

Comparative Label-Based Proteomics of Venoms from Echis ocellatus, Naja nigricollis, and Bitis arietans

Abdulbaki Alfa-Ibrahim Adio et al. Proteomes. .

Abstract

Background: Snake envenomation is a major public health issue in Nigeria, primarily due to bites from Echis ocellatus, Naja nigricollis, and Bitis arietans. Understanding their venom composition is essential for effective antivenom development. This study characterizes and compares the venom proteomes of these snakes using iTRAQ-based proteomics, focusing on key toxin families and their relative abundances. Methods: Venom samples were ethically collected from adult snakes, pooled by species, lyophilized, and stored for proteomic analysis. Proteins were extracted, digested with trypsin, and labeled with iTRAQ. Peptides were analyzed via mass spectrometry, and data were processed using Mascot and IQuant for protein identification and quantification. Results:E. ocellatus and B. arietans venoms had similar profiles, rich in C-type lectins, serine proteases, and phospholipase A2s. These comprised 17%, 11%, and 5% in E. ocellatus and 47%, 10%, and 7% in B. arietans, with metalloproteinases dominating both (53% and 47%). In N. nigricollis, three-finger toxins (9%) were most abundant, followed by metalloproteinases (3%). All species shared four core protein families, with N. nigricollis also containing four uncharacterized proteins. Conclusions: This study highlights venom compositional differences, advancing snake venom biology and informing targeted antivenom development.

Keywords: antivenom development; envenomation; iTRAQ; mass spectrometry; proteomics; snake venom.

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Conflict of interest statement

The authors report no declarations of interest.

Figures

Figure 1
Figure 1
Schematic experimental workflow.
Figure 2
Figure 2
One-dimensional SDS-PAGE profile of N. nigricollis, E. ocellatus and B. arietans.
Figure 3
Figure 3
Comparison of the identified protein families across the three snake species.
Figure 4
Figure 4
Relative distribution of (A) B. arietans, (B) E. ocellatus and (C) N. nigricollis venom protein families based on protein sequence coverage. GAP: glutamyl aminopeptidase; PLA2s: phospholipases A2; VNGF: venom nerve growth factor; SVSPs: snake venom serine proteases; VEGF: venom endothelial growth factor; KUNPI: Kunitz-type protease inhibitor; GAP: glutamyl aminopeptidase; LAAO: L-amino acid oxidase; SVMs: snake venom metalloproteinases; CRISP: cysteine-rich secretory protein; PIs: protease inhibitors; VP: venom phosphodiesterase; RPs: ribosomal proteins; PLB: phospholipase B; GC: glutaminyl cyclase; GRPs: glucose-regulated proteins; V5NTD: venom 5′-nucleotidases; GP: glutathione peroxidase; RDH: retinol dehydrogenase; 3FTXs: three-finger toxins; CVF: cobra venom factor.
Figure 4
Figure 4
Relative distribution of (A) B. arietans, (B) E. ocellatus and (C) N. nigricollis venom protein families based on protein sequence coverage. GAP: glutamyl aminopeptidase; PLA2s: phospholipases A2; VNGF: venom nerve growth factor; SVSPs: snake venom serine proteases; VEGF: venom endothelial growth factor; KUNPI: Kunitz-type protease inhibitor; GAP: glutamyl aminopeptidase; LAAO: L-amino acid oxidase; SVMs: snake venom metalloproteinases; CRISP: cysteine-rich secretory protein; PIs: protease inhibitors; VP: venom phosphodiesterase; RPs: ribosomal proteins; PLB: phospholipase B; GC: glutaminyl cyclase; GRPs: glucose-regulated proteins; V5NTD: venom 5′-nucleotidases; GP: glutathione peroxidase; RDH: retinol dehydrogenase; 3FTXs: three-finger toxins; CVF: cobra venom factor.
Figure 5
Figure 5
Mass distribution of identified proteins across the three snake species.
Figure 6
Figure 6
Distribution of unique peptide number across the three snake species.
Figure 7
Figure 7
Protein coverage distribution of the identified proteins across the three snake species.

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