Plectreurys tristis venome: A proteomic and transcriptomic analysis.

Area of Science:

• Arachnology
• Venomics
• Biochemistry

Background:

• Spider venoms are complex mixtures of bioactive molecules.
• Plectreurys tristis spiders possess unique venom gland structures and a primitive phylogenetic position.
• Previous studies identified plectoxins (PLTX) and bis(agmatine)oxalamide in P. tristis venom.

Purpose of the Study:

• To partially characterize the venome of Plectreurys tristis using integrated transcriptomic and proteomic approaches.
• To identify novel venom components and understand their functional significance.
• To investigate the evolutionary relationships of venom proteins with other arthropod species.

Main Methods:

• Combined transcriptomic and proteomic analyses of P. tristis venom glands and crude venom.
• Identification and classification of venom peptides and proteins.
• Comparative analysis of venom components with known databases.

Main Results:

• Discovery of six new groups of potential neurotoxins (U4-U9-PLTX), expanding known plectoxin families.
• Identification of known neurotoxins (U1-PLTX-Pt1a, U3-PLTX-Pt1a) and astacin metalloproteases.
• Venom composition is dominated by peptides and metalloproteases (94%), with a novel protein comprising 6% of the crude venom.
• Transcriptomic data revealed conserved gene families with homology to scorpion, spider, and tick proteins.
• Crude venom exhibits significant neurotoxic and paralytic activity in crickets, with an effective paralytic dose of 3.3µg/gm.

Conclusions:

• The venome of P. tristis is a rich source of diverse neurotoxic peptides and functional proteins.
• Integrated omics approaches are effective for characterizing complex venoms.
• P. tristis venom components show evolutionary links to other arthropod venoms and secretions.
• The identified neurotoxins and proteins contribute to the venom's potent paralytic effects.