Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia
ABSTRACT: Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panama, Colombia, and Ecuador, whose venom is poorly characterized. In the ́ present work, the protein composition of this venom was profiled using the ‘snake venomics’ analytical strategy. Decomplexation of...
- Autores:
-
Fernández Culma, Maritza
Pereañez Jiménez, Jaime Andrés
Núñez Rangel, Vitelbina
Lomonte, Bruno
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2014
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/36220
- Acceso en línea:
- https://hdl.handle.net/10495/36220
- Palabra clave:
- Venenos de Serpiente
Snake Venoms
Viperidae
Proteómica
Proteomics
Colombia
Ecuador
Panamá
Mordeduras de Serpientes
Snake Bites
Bothrops punctatus
- Rights
- openAccess
- License
- https://creativecommons.org/licenses/by/4.0/
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Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| title |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| spellingShingle |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia Venenos de Serpiente Snake Venoms Viperidae Proteómica Proteomics Colombia Ecuador Panamá Mordeduras de Serpientes Snake Bites Bothrops punctatus |
| title_short |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| title_full |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| title_fullStr |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| title_full_unstemmed |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| title_sort |
Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia |
| dc.creator.fl_str_mv |
Fernández Culma, Maritza Pereañez Jiménez, Jaime Andrés Núñez Rangel, Vitelbina Lomonte, Bruno |
| dc.contributor.author.none.fl_str_mv |
Fernández Culma, Maritza Pereañez Jiménez, Jaime Andrés Núñez Rangel, Vitelbina Lomonte, Bruno |
| dc.contributor.researchgroup.spa.fl_str_mv |
Toxinología, Alternativas Terapéuticas y Alimentarias |
| dc.subject.decs.none.fl_str_mv |
Venenos de Serpiente Snake Venoms Viperidae Proteómica Proteomics Colombia Ecuador Panamá Mordeduras de Serpientes Snake Bites |
| topic |
Venenos de Serpiente Snake Venoms Viperidae Proteómica Proteomics Colombia Ecuador Panamá Mordeduras de Serpientes Snake Bites Bothrops punctatus |
| dc.subject.proposal.spa.fl_str_mv |
Bothrops punctatus |
| description |
ABSTRACT: Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panama, Colombia, and Ecuador, whose venom is poorly characterized. In the ́ present work, the protein composition of this venom was profiled using the ‘snake venomics’ analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses. |
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2014 |
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2014 |
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2023-08-15T19:34:04Z |
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2023-08-15T19:34:04Z |
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Artículo de investigación |
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Fernandez Culma et al. (2014), Snake venomics of ́ Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia. PeerJ 2:e246; DOI 10.7717/peerj.246 |
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2167-8359 |
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https://hdl.handle.net/10495/36220 |
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Fernandez Culma et al. (2014), Snake venomics of ́ Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia. PeerJ 2:e246; DOI 10.7717/peerj.246 2167-8359 10.7717/peerj.246 |
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Fernández Culma, MaritzaPereañez Jiménez, Jaime AndrésNúñez Rangel, VitelbinaLomonte, BrunoToxinología, Alternativas Terapéuticas y Alimentarias2023-08-15T19:34:04Z2023-08-15T19:34:04Z2014Fernandez Culma et al. (2014), Snake venomics of ́ Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia. PeerJ 2:e246; DOI 10.7717/peerj.2462167-8359https://hdl.handle.net/10495/3622010.7717/peerj.246ABSTRACT: Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panama, Colombia, and Ecuador, whose venom is poorly characterized. In the ́ present work, the protein composition of this venom was profiled using the ‘snake venomics’ analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.COL001447616application/pdfengPeerJCorte Madera, Estados Unidoshttps://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/2.5/co/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Snake venomics of Bothrops punctatus, a semiarboreal pitviper species from Antioquia, ColombiaArtículo de investigaciónhttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARThttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionVenenos de SerpienteSnake VenomsViperidaeProteómicaProteomicsColombiaEcuadorPanamáMordeduras de SerpientesSnake BitesBothrops punctatusPeerJ.1624612PeerJPublicationCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927https://bibliotecadigital.udea.edu.co/bitstreams/bb58602a-9042-4922-952c-1a61d0669a76/download1646d1f6b96dbbbc38035efc9239ac9cMD52falseAnonymousREADLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bibliotecadigital.udea.edu.co/bitstreams/cfb35827-5051-4b51-a8ff-22a8cd360305/download8a4605be74aa9ea9d79846c1fba20a33MD53falseAnonymousREADORIGINALFernandezMaritza_2014_Snake_Venomics.pdfFernandezMaritza_2014_Snake_Venomics.pdfArtículo de investigaciónapplication/pdf1689860https://bibliotecadigital.udea.edu.co/bitstreams/241b8803-922c-4143-97c2-99487e04ed39/download26ac56ef982b10659c16c3520c073b93MD51trueAnonymousREADTEXTFernandezMaritza_2014_Snake_Venomics.pdf.txtFernandezMaritza_2014_Snake_Venomics.pdf.txtExtracted texttext/plain44171https://bibliotecadigital.udea.edu.co/bitstreams/44e5895d-cdea-4f80-af0a-dee3958212bf/downloadda0686e2470329ee329bbff5ca969b92MD54falseAnonymousREADTHUMBNAILFernandezMaritza_2014_Snake_Venomics.pdf.jpgFernandezMaritza_2014_Snake_Venomics.pdf.jpgGenerated Thumbnailimage/jpeg14562https://bibliotecadigital.udea.edu.co/bitstreams/aaf878ef-bbc1-4943-841a-474c085a0ea3/downloada1193b4a3d0e346afae99933fe87a4d2MD55falseAnonymousREAD10495/36220oai:bibliotecadigital.udea.edu.co:10495/362202025-03-26 21:20:57.8https://creativecommons.org/licenses/by/4.0/open.accesshttps://bibliotecadigital.udea.edu.coRepositorio Institucional de la Universidad de Antioquiaaplicacionbibliotecadigitalbiblioteca@udea.edu.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 |
