A survey of the venom of the spider Lycosa vittata by biochemical, pharmacological and transcriptomic analyses

Abstract

Lycosa vittata, mainly distributed in the southwest of China, is a medium-sized and venomous spider, whose venom remains unexplored so far. This study aims to present an overview of the venom. It mainly consisted of diverse peptides and exhibited inhibitory effects on voltage-gated ion channels in rat dorsal root ganglia neurons, with a strongest inhibition on tetrodotoxin-sensitive and tetrodotoxin-resistant voltage-gated Na(+) channels. Interestingly, it exerted cytotoxicity to cancer cells, with approximately 10-fold selectivity on PC-3 over others, implying the existence of selective anti-PC-3 agents in the venom. Moreover, 51 toxin-like peptides were deduced from the venom gland transcriptome. Bioinformatic analyses suggested their structures might have some distinguished properties and their predicted functions were consistent with the venom activities. This study suggests that the venom is an attractive source of neurotoxins with therapeutic significance, and provides references for the structure and function investigation of specific toxins in the future.

An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches

“…Normally, spider toxins are reported as having a conserved gene structure as well as precursor organization; being composed of three segments that include signal peptide, propeptide, and mature peptide [ 83 ]. Although it is not common, toxin precursors lacking propeptide have been reported in some spider transcriptomes [ 49 , 52 , 84 , 85 ]. In addition, according to their cysteine framework, sequences from groups III and IV are not predicted to adopt the ICK structural motif, presenting an unknown folding ( Table 2 ).…”

The role of weak interactions in characterizing peptide folding preferences using a QTAIM interpretation of the Ramachandran plot (ϕ‐ψ)

“… The topological complexity Σ brc and relative energy Δ Ε (computed with DFT/ωB97XD/6–31 + g) for the molecular graphs of the five conformers of lycosin, see Supporting Information Figure S1 . The α‐helix structure lycosin peptide with the 24 amino acid sequence RKGWFKAMKSIAKFIAKEKLKEHL …”

Spider Transcriptomes from Venom Glands: Molecular Diversity of Ion Channel Toxins and Antimicrobial Peptide Transcripts

“…Some authors used female spiders as source of venom gland for the RNA extraction, (see Table 1, e.g., L. vittata, A. ventricosus). The transcriptome analysis of the spider L. vittata was generated from venom glands of six adult female spiders (Zhang et al 2015). The authors did not mention previously venom milking on specimens used in the library construction.…”

“…The authors did not mention previously venom milking on specimens used in the library construction. However, the authors selected approximately 500 clones from the cDNA library to obtain 51 toxin-like peptide precursors (Zhang et al 2015).…”

“…In Russia, Dolomedes fimbriatus was described by Sergey Kozlov (Kozlov et al 2014). Transcriptome from L. vittata was published by the group of Zhonghua Liu (Zhang et al 2015). Songping Liang (in China) and collaborators reported transcriptomes from Chilobrachys jingzhao , Haplopelma schmidti also known as Ornithoctonus huwena , Lycosa singoriensis ), H. hainanum or O. hainana , Araneus ventricosus , and Dolomedes mizhoanus venom gland transcriptomes: Glenn King (Australia) and his group generated the transcriptome from Selenotypus plumipes using the Roche 454 GS FLX platform (Wong et al 2013).…”