Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach
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 <i>Pamphobeteus verdolaga</i>. We...
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doaj-9a3f32c305834f00b9d156b7d85f91b72021-07-23T14:09:56ZengMDPI AGToxins2072-66512021-06-011345345310.3390/toxins13070453Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID ApproachSebastian Estrada-Gómez0Leidy Johana Vargas-Muñoz1Cesar Segura Latorre2Monica Maria Saldarriaga-Cordoba3Claudia Marcela Arenas-Gómez4Grupo de Toxinología—Serpentario, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Carrera 53 No. 61-30, Medellín 050010, ColombiaFacultad de Medicina, Universidad Cooperativa de Colombia, Calle 50 A No. 41-20, Medellín 050012, ColombiaGrupo de Toxinología—Serpentario, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Carrera 53 No. 61-30, Medellín 050010, ColombiaCentro de Investigación en Recursos Naturales y Sustentabilidad, Universidad Bernardo O’Higgins, Avenida Viel 1497, Santiago 7750000, ChileGrupo de Génetica, Regeneración y Cáncer, Universidad de Antioquia UdeA, Carrera 53 No. 61-30, Medellín 050010, ColombiaNowadays, 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 <i>Pamphobeteus verdolaga</i>. 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<sub>2</sub>, 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 <i>P. verdolaga</i> includes a basal protein that underwent a duplication event that gave origin to the lycotoxin proteins reported for <i>Lycosa sp.</i> This approach allows proposing an evolutionary relationship of high-molecular-mass proteins among <i>P. verdolaga</i> and other spider species.https://www.mdpi.com/2072-6651/13/7/453Theraphosidae<i>Pamphobeteus</i>transcriptomichigh-molecular-mass compoundsphospholipaseskunitz-type |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sebastian Estrada-Gómez Leidy Johana Vargas-Muñoz Cesar Segura Latorre Monica Maria Saldarriaga-Cordoba Claudia Marcela Arenas-Gómez |
spellingShingle |
Sebastian Estrada-Gómez Leidy Johana Vargas-Muñoz Cesar Segura Latorre Monica Maria Saldarriaga-Cordoba Claudia Marcela Arenas-Gómez Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach Toxins Theraphosidae <i>Pamphobeteus</i> transcriptomic high-molecular-mass compounds phospholipases kunitz-type |
author_facet |
Sebastian Estrada-Gómez Leidy Johana Vargas-Muñoz Cesar Segura Latorre Monica Maria Saldarriaga-Cordoba Claudia Marcela Arenas-Gómez |
author_sort |
Sebastian Estrada-Gómez |
title |
Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach |
title_short |
Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach |
title_full |
Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach |
title_fullStr |
Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach |
title_full_unstemmed |
Analysis of High Molecular Mass Compounds from the Spider <i>Pamphobeteus verdolaga</i> Venom Gland. A Transcriptomic and MS ID Approach |
title_sort |
analysis of high molecular mass compounds from the spider <i>pamphobeteus verdolaga</i> venom gland. a transcriptomic and ms id approach |
publisher |
MDPI AG |
series |
Toxins |
issn |
2072-6651 |
publishDate |
2021-06-01 |
description |
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 <i>Pamphobeteus verdolaga</i>. 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<sub>2</sub>, 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 <i>P. verdolaga</i> includes a basal protein that underwent a duplication event that gave origin to the lycotoxin proteins reported for <i>Lycosa sp.</i> This approach allows proposing an evolutionary relationship of high-molecular-mass proteins among <i>P. verdolaga</i> and other spider species. |
topic |
Theraphosidae <i>Pamphobeteus</i> transcriptomic high-molecular-mass compounds phospholipases kunitz-type |
url |
https://www.mdpi.com/2072-6651/13/7/453 |
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