Abstract
Nowadays, spider venom research focuses on the neurotoxic activity of small peptides. In this study, we investigated high-molecular-mass compounds that have either enzymatic activity or housekeeping functions present in either the venom gland or venom of Pamphobeteus verdolaga. We used proteomic and transcriptomic-assisted approaches to recognize the proteins sequences related to high-molecular-mass compounds present in either venom gland or venom. We report the amino acid sequences (partial or complete) of 45 high-molecular-mass compounds detected by transcriptomics showing similarity to other proteins with either enzymatic activity (i.e., phospholipases A2, kunitz-type, hyaluronidases, and sphingomyelinase D) or housekeeping functions involved in the signaling process, glucanotransferase function, and beta-N-acetylglucosaminidase activity. MS/MS analysis showed fragments exhibiting a resemblance similarity with different sequences detected by transcriptomics corresponding to sphingomyelinase D, hyaluronidase, lycotoxins, cysteine-rich secretory proteins, and kunitz-type serine protease inhibitors, among others. Additionally, we report a probably new protein sequence corresponding to the lycotoxin family detected by transcriptomics. The phylogeny analysis suggested that P. verdolaga includes a basal protein that underwent a duplication event that gave origin to the lycotoxin proteins reported for Lycosa sp. This approach allows proposing an evolutionary relationship of high-molecular-mass proteins among P. verdolaga and other spider species.
Highlights
Spider venom is a complex mixture of pharmacologically active peptides, proteins, and inorganic compounds
In the venom gland transcriptome of P. verdolaga, we identified 45 transcripts coding for the putative protein ORFs previously reported, corresponding to phospholipases A2, phospholipases D, phospholipases B, kunitz-type serine protease inhibitors (KTSPI), hyaluronidases, lycotoxins toxins, cysteine-rich secretory proteins (CRISPs) proteins, hephaestin-like protein and venom metalloproteinase
In the P. verdolaga venom gland transcriptome, we found 13 contigs encoding members of the less common family of venom proteins known as kunitz-type serine protease inhibitors (KTSPI)
Summary
Spider venom is a complex mixture of pharmacologically active peptides, proteins, and inorganic compounds. Most spider venom toxins can be classified into one of three groups, depending on their molecular mass i.e., low (10 kDa) [1]. The vast majority of transcriptomic and proteomic analyses have focused on medium-molecular-mass peptides, since these compounds are the main ones responsible for the toxic effects produced by spider venoms (except in the Theridiidae family). High-molecular-mass compounds (HMMC) are more commonly distributed among spider venoms than is described in the literature [1]. Most of the HMMC reported correspond to proteins with housekeeping activity, and venom proteins with enzymatic activities have been described in the Theraphosidae species Ornithoctonus huwena, Grammostola iheringi, Chilobrachys jingzhao, Haplopelma hainanum, and Haplopelma schmidti [2,3,4,5,6]. The primary role of these compounds is the degradation of the extracellular matrix (collagenase, hyaluronidase, and proteases) and the underlying cell membrane [1]
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