Analysis of high molecular mass compounds from the spider pamphobeteus verdolaga venom gland. A transcriptomic and MS ID approach
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 pro...
- Autores:
-
Estrada Gómez, Sebastián
Segura Latorre, Cesar
Arenas Gómez, Claudia Marcela
Vargas Muñoz, Leidy Johana
Saldarriaga Córdoba, Monica María
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2021
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/41071
- Acceso en línea:
- https://hdl.handle.net/10495/41071
- Palabra clave:
- Secuencia de Aminoácidos
Amino Acid Sequence
Proteínas de Artrópodos - análisis
Arthropod Proteins - analysis
Proteínas de Artrópodos - química
Arthropod Proteins - chemistry
Glándulas Exocrinas - química
Exocrine Glands - chemistry
Peso Molecular
Molecular Weight
Proteoma
Proteome
Venenos de Araña
Spider Venoms
Arañas
Spiders
Espectrometría de Masas en Tándem
Tandem Mass Spectrometry
Transcriptoma
Transcriptome
https://id.nlm.nih.gov/mesh/D000595
https://id.nlm.nih.gov/mesh/D060829
https://id.nlm.nih.gov/mesh/D005088
https://id.nlm.nih.gov/mesh/D008970
https://id.nlm.nih.gov/mesh/D020543
https://id.nlm.nih.gov/mesh/D013111
https://id.nlm.nih.gov/mesh/D013112
https://id.nlm.nih.gov/mesh/D053719
https://id.nlm.nih.gov/mesh/D059467
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by/2.5/co/
| Summary: | 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. |
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