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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Main Authors: Sebastian Estrada-Gómez, Leidy Johana Vargas-Muñoz, Cesar Segura Latorre, Monica Maria Saldarriaga-Cordoba, Claudia Marcela Arenas-Gómez
Format: Article
Language:English
Published: MDPI AG 2021-06-01
Series:Toxins
Subjects:
Online Access:https://www.mdpi.com/2072-6651/13/7/453
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spelling 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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