Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach

• Published in: Toxins 2021-06, Vol.13 (7), p.453
• Main Authors: Estrada-Gómez, Sebastian, Vargas-Muñoz, Leidy Johana, Segura Latorre, Cesar, Saldarriaga-Cordoba, Monica Maria, Arenas-Gómez, Claudia Marcela
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Animals; Arthropod Proteins - analysis; Arthropod Proteins - chemistry; Enzymatic activity; Exocrine Glands - chemistry; high-molecular-mass compounds; kunitz-type; Molecular Weight; N-Acetylglucosaminidase; Neurotoxicity; Pamphobeteus; Peptides; phospholipases; Phylogenetics; Phylogeny; Protease inhibitors; Proteinase inhibitors; Proteins; Proteome; Proteomics; Serine; Serine proteinase; Similarity; Sphingomyelin phosphodiesterase; Spider Venoms - analysis; Spider Venoms - chemistry; Spider Venoms - genetics; Spiders; Tandem Mass Spectrometry; Theraphosidae; Toxins; Transcriptome; transcriptomic; Venom gland
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins13070453

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 . 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 A , 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 includes a basal protein that underwent a duplication event that gave origin to the lycotoxin proteins reported for This approach allows proposing an evolutionary relationship of high-molecular-mass proteins among and other spider species.