Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga 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 Pamphobeteus verdolaga. We used proteomic and...
- Autores:
-
Sebastian Estrada-Gómez, Leidy Johana Vargas-Muñoz
Cesar Segura Latorre, Monica Maria Saldarriaga-Cordoba
Claudia Marcela Arenas-Gómez
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2021
- Institución:
- Universidad Cooperativa de Colombia
- Repositorio:
- Repositorio UCC
- Idioma:
- OAI Identifier:
- oai:repository.ucc.edu.co:20.500.12494/45800
- Acceso en línea:
- https://hdl.handle.net/20.500.12494/45800
- Palabra clave:
- Theraphosidae
high-molecular-mass compounds
Pamphobeteus; transcriptomic
phospholipases
kunitz-type
hyaluronidases
lycotoxins
- Rights
- closedAccess
- License
- Atribución
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| dc.title.spa.fl_str_mv |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| title |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| spellingShingle |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach Theraphosidae high-molecular-mass compounds Pamphobeteus; transcriptomic phospholipases kunitz-type hyaluronidases lycotoxins |
| title_short |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| title_full |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| title_fullStr |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| title_full_unstemmed |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| title_sort |
Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach |
| dc.creator.fl_str_mv |
Sebastian Estrada-Gómez, Leidy Johana Vargas-Muñoz Cesar Segura Latorre, Monica Maria Saldarriaga-Cordoba Claudia Marcela Arenas-Gómez |
| dc.contributor.author.none.fl_str_mv |
Sebastian Estrada-Gómez, Leidy Johana Vargas-Muñoz Cesar Segura Latorre, Monica Maria Saldarriaga-Cordoba Claudia Marcela Arenas-Gómez |
| dc.subject.spa.fl_str_mv |
Theraphosidae high-molecular-mass compounds Pamphobeteus; transcriptomic phospholipases kunitz-type hyaluronidases lycotoxins |
| topic |
Theraphosidae high-molecular-mass compounds Pamphobeteus; transcriptomic phospholipases kunitz-type hyaluronidases lycotoxins |
| 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 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. |
| publishDate |
2021 |
| dc.date.issued.none.fl_str_mv |
2021-06-29 |
| dc.date.accessioned.none.fl_str_mv |
2022-07-19T20:28:04Z |
| dc.date.available.none.fl_str_mv |
2022-07-19T20:28:04Z |
| dc.type.none.fl_str_mv |
Artículos Científicos |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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info:eu-repo/semantics/article |
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info:eu-repo/semantics/publishedVersion |
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20726651 |
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doi.org/10.3390/toxins13070453 |
| dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/20.500.12494/45800 |
| dc.identifier.bibliographicCitation.spa.fl_str_mv |
Estrada-Gómez S, Vargas-Muñoz LJ, Segura Latorre C, Saldarriaga-Cordoba MM, Arenas-Gómez CM. Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach. Toxins (Basel). 2021 Jun 29;13(7):453. doi: 10.3390/toxins13070453. PMID: 34209760; PMCID: PMC8309857. |
| identifier_str_mv |
20726651 doi.org/10.3390/toxins13070453 Estrada-Gómez S, Vargas-Muñoz LJ, Segura Latorre C, Saldarriaga-Cordoba MM, Arenas-Gómez CM. Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach. Toxins (Basel). 2021 Jun 29;13(7):453. doi: 10.3390/toxins13070453. PMID: 34209760; PMCID: PMC8309857. |
| url |
https://hdl.handle.net/20.500.12494/45800 |
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https://pubmed.ncbi.nlm.nih.gov/34209760/ |
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Toxins |
| dc.relation.references.spa.fl_str_mv |
King, G.F.; Hardy, M.C. Spider-venom peptides: Structure, pharmacology, and potential for control of insect pests. Annu. Rev. Entomol. 2013, 58, 475–496. [CrossRef] [PubMed] Cheng, T.C.; Long, R.W.; Wu, Y.Q.; Guo, Y.B.; Liu, D.L.; Peng, L.; Li, D.Q.; Yang, D.W.; Xu, X.; Liu, F.X.; et al. Identification and characterization of toxins in the venom gland of the Chinese bird spider, Haplopelma hainanum, by transcriptomic analysis. Insect Sci. 2016, 23, 487–499. [CrossRef] [PubMed] Jiang, L.; Peng, L.; Chen, J.; Zhang, Y.; Xiong, X.; Liang, S. Molecular diversification based on analysis of expressed sequence tags from the venom glands of the Chinese bird spider Ornithoctonus huwena. Toxicon 2008, 51, 1479–1489. [CrossRef] Yuan, C.; Jin, Q.; Tang, X.; Hu, W.; Cao, R.; Yang, S.; Xiong, J.; Xie, C.; Xie, J.; Liang, S. Proteomic and peptidomic characterization of the venom from the Chinese bird spider, Ornithoctonus huwena Wang. J. Proteome Res. 2007, 6, 2792–2801. [CrossRef] Borges, M.H.; Figueiredo, S.G.; Leprevost, F.V.; De Lima, M.E.; Cordeiro Mdo, N.; Diniz, M.R.; Moresco, J.; Carvalho, P.C.; Yates, J.R. Venomous extract protein profile of Brazilian tarantula Grammostola iheringi: Searching for potential biotechnological applications. J. Proteom. 2016, 136, 35–47. [CrossRef] Liao, Z.; Cao, J.; Li, S.; Yan, X.; Hu, W.; He, Q.; Chen, J.; Tang, J.; Xie, J.; Liang, S. Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao. Proteomics 2007, 7, 1892–1907. [CrossRef] Cifuentes, Y.; Estrada-Gomez, S.; Vargas Munoz, L.J.; Perafan, C. Description and molecular characterization of a new species of tarantula, Pamphobeteus verdolaga, from Colombia (Aranae: Mygalomorphae: Theraphosidae). Zoologia 2016, 33. [CrossRef] Estrada-Gomez, S.; Vargas Munoz, L.J.; Quintana Castillo, J.C. Extraction and partial characterization of venom from the Colombian spider Pamphobeteus aff. nigricolor (Aranae:Theraphosidae). Toxicon 2013, 76C, 301–309. [CrossRef] [PubMed] Estrada-Gomez, S.; Vargas-Munoz, L.J.; Saldarriaga-Cordoba, M.; Cifuentes, Y.; Perafan, C. Identifying different transcribed proteins in the newly described Theraphosidae Pamphobeteus verdolaga. Toxicon 2017, 129, 81–88. [CrossRef] [PubMed] Estrada-Gomez, S.; Caldas Cardoso, F.; Vargas-Munoz, L.J.; Quintana-Castillo, J.C.; Arenas Gomez, C.M.; Pineda, S.S. Venomic, transcriptomic, and bioactivity analyses of Pamphobeteus verdolaga venom reveal complex disulfide-rich peptides that modulate calcium channels. Toxins 2019, 11, 4 Clement, H.; Olvera, A.; Rodriguez, M.; Zamudio, F.; Palomares, L.A.; Possani, L.D.; Odell, G.V.; Alagon, A.; Sanchez-Lopez, R. Identification, cDNA cloning and heterologous expression of a hyaluronidase from the tarantula Brachypelma vagans venom. Toxicon 2012, 60, 1223–1227 . Ortiz, E.; Gurrola, G.B.; Schwartz, E.F.; Possani, L.D. Scorpion venom components as potential candidates for drug development. Toxicon 2015, 93, 125–135. [C Vargas Munoz, L.J.; Estrada-Gomez, S. Purification and Characterization of Venom Components as Source for Antibiotics. Mini-Rev. Org. Chem. 2014, 11, 15–27. [C Vargas Munoz, L.J.; Estrada-Gomez, S.; Escobar, J. Snake and scorpion toxins venoms, a natural source of molecules with antimicrobial activity. Curare 2015, 2. Kini, R.M. Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms. Toxicon 2005, 45, 1147–1161 Zhu, H.; Dupureur, C.M.; Zhang, X.; Tsai, M.D. Phospholipase A2 engineering. The roles of disulfide bonds in structure, conformational stability, and catalytic function. Biochemistry 1995, 34, 15307–15314. Ho, I.C.; Arm, J.P.; Bingham, C.O., 3rd; Choi, A.; Austen, K.F.; Glimcher, L.H. A novel group of phospholipase A2s preferentially expressed in type 2 helper T cells. J. Biol. Chem. 2001, 276, 18321–18326 Haney, R.A.; Clarke, T.H.; Gadgil, R.; Fitzpatrick, R.; Hayashi, C.Y.; Ayoub, N.A.; Garb, J.E. Effects of Gene Duplication, Positive Selection, and Shifts in Gene Expression on the Evolution of the Venom Gland Transcriptome in Widow Spiders. Genome Biol. Evol. 2016, 8, 228–242. [ Dantas, A.E.; Carmo, A.O.; Horta, C.C.; Leal, H.G.; Oliveira-Mendes, B.B.; Martins, A.P.; Chavez-Olortegui, C.; Kalapothakis, E. Description of Loxtox protein family and identification of a new group of Phospholipases D from Loxosceles similis venom gland. Toxicon 2016, 120, 97–106 Chaves-Moreira, D.; Souza, F.N.; Fogaça, R.T.; Mangili, O.C.; Gremski, W.; Senff-Ribeiro, A.; Chaim, O.M.; Veiga, S.S. The relationship between calcium and the metabolism of plasma membrane phospholipids in hemolysis induced by brown spider venom phospholipase-D toxin. J. Cell. Biochem. 2011, 112, 2529–2540 Yao, Y.; Li, J.; Lin, Y.; Zhou, J.; Zhang, P.; Xu, Y. Structural insights into phospholipase D function. Prog. Lipid Res. 2021, 81, 101070. Kudo, I.; Murakami, M. Phospholipase A2 enzymes. Prostaglandins Other Lipid Mediat. 2002, 68–69, 3–58. [C Earl, S.T.H.; Richards, R.; Johnson, L.A.; Flight, S.; Anderson, S.; Liao, A.; De Jersey, J.; Masci, P.P.; Lavin, M.F. Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms. Biochimie 2012, 94, 365–373 Mukherjee, A.K.; Mackessy, S.P.; Dutta, S. Characterization of a Kunitz-type protease inhibitor peptide (Rusvikunin) purified from Daboia russelii russelii venom. Int. J. Biol. Macromol. 2014, 67, 154–162 Qiu, Y.; Lee, K.S.; Choo, Y.M.; Kong, D.; Yoon, H.J.; Jin, B.R. Molecular cloning and antifibrinolytic activity of a serine protease inhibitor from bumblebee (Bombus terrestris) venom. Toxicon 2013, 63, 1–6 Chang, L.-s.; Chung, C.; Huang, H.-B.; Lin, S.-r. Purification and Characterization of a Chymotrypsin Inhibitor from the Venom of Ophiophagus hannah (King Cobra). Biochem. Biophys. Res. Commun. 2001, 283, 862–867. [C Yang, X.; Wang, Y.; Lu, Z.; Zhai, L.; Jiang, J.; Liu, J.; Yu, H. A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius. Comp. Biochem. Physiol. Part B Biochem. Mol. Biol. 2009, 153, 116–120. [C . Wan, H.; Lee, K.S.; Kim, B.Y.; Zou, F.M.; Yoon, H.J.; Je, Y.H.; Li, J.; Jin, B.R. A spider-derived Kunitz-type serine protease inhibitor that acts as a plasmin inhibitor and an elastase inhibitor. PLoS ONE 2013, 8, e53343 Tang, X.; Zhang, Y.; Hu, W.; Xu, D.; Tao, H.; Yang, X.; Li, Y.; Jiang, L.; Liang, S. Molecular diversification of peptide toxins from the tarantula Haplopelma hainanum (Ornithoctonus hainana) venom based on transcriptomic, peptidomic, and genomic analyses. J. Proteome Res. 2010, 9, 2550–2564. Yuan, C.H.; He, Q.Y.; Peng, K.; Diao, J.B.; Jiang, L.P.; Tang, X.; Liang, S.P. Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas. PLoS ONE 2008, 3, e3414. Undheim, E.A.; Sunagar, K.; Herzig, V.; Kely, L.; Low, D.H.; Jackson, T.N.; Jones, A.; Kurniawan, N.; King, G.F.; Ali, S.A.; et al. A proteomics and transcriptomics investigation of the venom from the barychelid spider Trittame loki (brush-foot trapdoor). Toxins 2013, 5, 2488–2503 Zweckstetter, M.; Czisch, M.; Mayer, U.; Chu, M.L.; Zinth, W.; Timpl, R.; Holak, T.A. Structure and multiple conformations of the kunitz-type domain from human type VI collagen alpha3(VI) chain in solution. Structure 1996, 4, 195–209. [C He, Q.; Duan, Z.; Yu, Y.; Liu, Z.; Liu, Z.; Liang, S. The venom gland transcriptome of Latrodectus tredecimguttatus revealed by deep sequencing and cDNA library analysis. PLoS ONE 2013, 8, e81357. Kumar, S.; Stecher, G.; Suleski, M.; Hedges, S.B. TimeTree: A Resource for Timelines, Timetrees, and Divergence Times. Mol. Biol. Evol. 2017, 34, 1812–1819. Yan, L.; Adams, M.E. 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[ Zhang, B.; Liu, Q.; Yin, W.; Zhang, X.; Huang, Y.; Luo, Y.; Qiu, P.; Su, X.; Yu, J.; Hu, S.; et al. Transcriptome analysis of Deinagkistrodon acutus venomous gland focusing on cellular structure and functional aspects using expressed sequence tags. BMC Genom. 2006, 7, 152 Liang, S. Proteome and peptidome profiling of spider venoms. Expert Rev. Proteom. 2008, 5, 731–746 Duan, Z.G.; Yan, X.J.; He, X.Z.; Zhou, H.; Chen, P.; Cao, R.; Xiong, J.X.; Hu, W.J.; Wang, X.C.; Liang, S.P. Extraction and protein component analysis of venom from the dissected venom glands of Latrodectus tredecimguttatus. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2006, 145, 350–357 Gething, M.-J.; Sambrook, J. Protein folding in the cell. Nature 1992, 355, 33–45 Fernandes-Pedrosa Mde, F.; Junqueira-de-Azevedo Ide, L.; Gonçalves-de-Andrade, R.M.; Kobashi, L.S.; Almeida, D.D.; Ho, P.L.; Tambourgi, D.V. Transcriptome analysis of Loxosceles laeta (Araneae, Sicariidae) spider venomous gland using expressed sequence tags. BMC Genom. 2008, 9, 279. Laedermann, C.J.; Decosterd, I.; Abriel, H. Ubiquitylation of voltage-gated sodium channels. Handb. Exp. Pharmacol. 2014, 221, 231–250. Cui, Y.; Zhu, Y.; Lin, Y.; Chen, L.; Feng, Q.; Wang, W.; Xiang, H. New insight into the mechanism underlying the silk gland biological process by knocking out fibroin heavy chain in the silkworm. BMC Genom. 2018, 19, 215. [ Oukkache, N.; Chgoury, F.; Lalaoui, M.; Cano, A.A.; Ghalim, N. Comparison between two methods of scorpion venom milking in Morocco. J. Venom. Anim. Toxins Incl. Trop. Dis. 2013, 19, 5 World Health Organization. Progress in the Characterization of Venoms and Standardization of Antivenoms; WHO Offset Publication: Geneva, Switzerland, 1981; pp. 1–44. Fernandez, J.; Gutierrez, J.M.; Angulo, Y.; Sanz, L.; Juarez, P.; Calvete, J.J.; Lomonte, B. Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization. Biochimie 2010, 92, 273–283. . Herzig, V.; Wood, D.L.A.; Newell, F.; Chaumeil, P.-A.; Kaas, Q.; Binford, G.J.; Nicholson, G.M.; Gorse, D.; King, G.F. ArachnoServer 2.0, an updated online resource for spider toxin sequences and structures. Nucleic Acids Res. 2011, 39, D653–D657. [C UniProt. UniProt: The universal protein knowledgebase. Nucleic Acids Res. 2017, 45, D158–D169 NCBI. Database Resources of the National Center for Biotechnology Information. Nucleic Acids Res. 2017, 44, D7–D19. Goujon, M.; McWilliam, H.; Li, W.; Valentin, F.; Squizzato, S.; Paern, J.; Lopez, R. A new bioinformatics analysis tools framework at EMBL-EBI. Nucleic Acids Res. 2010, 38, W695–W699 Pearson, W.R. Finding Protein and Nucleotide Similarities with FASTA. Curr. Protoc. Bioinform. 2016, 53, 3–9. [ Nguyen, L.T.; Schmidt, H.A.; von Haeseler, A.; Minh, B.Q. IQ-TREE: A fast and effective stochastic algorithm for estimating maximum-likelihood phylogenies. Mol. Biol. Evol. 2015, 32, 268–274 Letunic, I.; Bork, P. Interactive Tree Of Life (iTOL) v4: Recent updates and new developments. Nucleic Acids Res. 2019, 47, W256–W259. [ King, G.F.; Gentz, M.C.; Escoubas, P.; Nicholson, G.M. A rational nomenclature for naming peptide toxins from spiders and other venomous animals. Toxicon 2008, 52, 264–276. Almagro Armenteros, J.J.; Tsirigos, K.D.; Sønderby, C.K.; Petersen, T.N.; Winther, O.; Brunak, S.; von Heijne, G.; Nielsen, H. SignalP 5.0 improves signal peptide predictions using deep neural networks. Nat. Biotechnol. 2019, 37, 420–423. Ceroni, A.; Passerini, A.; Vullo, A.; Frasconi, P. DISULFIND: A disulfide bonding state and cysteine connectivity prediction server. Nucleic Acids Res. 2006, 34, W177–W181. Ferrè, F.; Clote, P. Disulfide connectivity prediction using secondary structure information and diresidue frequencies. Bioinformatics 2005, 21, 2336–2346 Ferrè, F.; Clote, P. DiANNA: A web server for disulfide connectivity prediction. Nucleic Acids Res. 2005, 33, W230–W232 |
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Sebastian Estrada-Gómez, Leidy Johana Vargas-MuñozCesar Segura Latorre, Monica Maria Saldarriaga-CordobaClaudia Marcela Arenas-Gómez132022-07-19T20:28:04Z2022-07-19T20:28:04Z2021-06-2920726651doi.org/10.3390/toxins13070453https://hdl.handle.net/20.500.12494/45800Estrada-Gómez S, Vargas-Muñoz LJ, Segura Latorre C, Saldarriaga-Cordoba MM, Arenas-Gómez CM. Analysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach. Toxins (Basel). 2021 Jun 29;13(7):453. doi: 10.3390/toxins13070453. PMID: 34209760; PMCID: PMC8309857.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.https://orcid.org/0000-0003-1332-5106Infettareleidy.vargasmu@campusucc.edu.co1-22Universidad cooperativa de Colombia, sede Medellín, MedicinaMedicinaMedellínhttps://pubmed.ncbi.nlm.nih.gov/34209760/ToxinsKing, G.F.; Hardy, M.C. Spider-venom peptides: Structure, pharmacology, and potential for control of insect pests. Annu. Rev. Entomol. 2013, 58, 475–496. [CrossRef] [PubMed]Cheng, T.C.; Long, R.W.; Wu, Y.Q.; Guo, Y.B.; Liu, D.L.; Peng, L.; Li, D.Q.; Yang, D.W.; Xu, X.; Liu, F.X.; et al. Identification and characterization of toxins in the venom gland of the Chinese bird spider, Haplopelma hainanum, by transcriptomic analysis. Insect Sci. 2016, 23, 487–499. 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A Transcriptomic and MS ID ApproachArtículos Científicoshttp://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionAtribucióninfo:eu-repo/semantics/closedAccesshttp://purl.org/coar/access_right/c_14cbPublicationLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repository.ucc.edu.co/bitstreams/35bddf30-7500-4317-901f-62d6c53e66ac/download8a4605be74aa9ea9d79846c1fba20a33MD52ORIGINALAnalysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. A Transcriptomic and MS ID Approach.pdfAnalysis of High Molecular Mass Compounds from the Spider Pamphobeteus verdolaga Venom Gland. 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A Transcriptomic and MS ID Approach.pdf.txtExtracted texttext/plain74420https://repository.ucc.edu.co/bitstreams/838ec143-d793-4edc-83f9-13d005234355/downloadf654fdb3809b5b87da304d1b97f54461MD5420.500.12494/45800oai:repository.ucc.edu.co:20.500.12494/458002024-08-10 20:55:41.257open.accesshttps://repository.ucc.edu.coRepositorio Institucional Universidad Cooperativa de Colombiabdigital@metabiblioteca.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 |