Comparative proteomic analysis reveals functional and evolutionary diversity in five Montivipera snake venoms

Area of Science:

• Zoology
• Biochemistry
• Evolutionary Biology

Background:

• Proteomic characterization of snake venoms is crucial for evolutionary insights and identifying therapeutic compounds.
• Montivipera species from the Near and Middle East are understudied, with previous venom analyses yielding incomplete and conflicting data.

Purpose of the Study:

• To conduct a comprehensive proteomic analysis of five Montivipera species.
• To compare venom complexity and identify conserved and unique protein families.
• To establish a foundation for future functional and evolutionary research on Montivipera venoms.

Main Methods:

• Integrated proteomic approach using SDS-PAGE, RP-HPLC, and shotgun proteomics.
• Employing both trypsin and multi-enzymatic limited digestions for enhanced protein identification.
• Comparative analysis of venom proteomes from five Montivipera species and Macrovipera lebetina.

Main Results:

• Identified 129–179 proteins and peptides per Montivipera species, revealing remarkable venom complexity.
• Detected major protein families including metalloproteinases, phospholipases A2, serine proteases, C-type lectins, VEGFs, and disintegrins.
• Found 39 shared proteins across all five Montivipera species, alongside previously unidentified low-abundance protein families.

Conclusions:

• Montivipera venoms exhibit both conserved and unique protein profiles across species.
• Interspecific variations in toxin abundance suggest differences in envenomation strategies.
• This study provides a detailed proteomic framework for Montivipera venom research.