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Snake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite management.
J Proteomics. 2009 Mar 06; 72(2):227-40.JP

Abstract

The taxonomic status of the medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela, which has been classified as Bothrops colombiensis, remains incertae cedis. To help resolving this question, the venom proteome of B. colombiensis was characterized by reverse-phase HPLC fractionation followed by analysis of each chromatographic fraction by SDS-PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass spectrometry of tryptic peptides. The venom contained proteins belonging to 8 types of families. PI Zn(2+)-metalloproteinases and K49 PLA(2) molecules comprise over 65% of the venom proteins. Other venom protein families comprised PIII Zn(2+)-metalloproteinases (11.3%), D49 PLA(2)s (10.2%), l-amino acid oxidase (5.7%), the medium-sized disintegrin colombistatin (5.6%), serine proteinases (1%), bradykinin-potentiating peptides (0.8%), a DC-fragment (0.5%), and a CRISP protein (0.1%). A comparison of the venom proteomes of B. colombiensis and B. atrox did not support the suggested synonymy between these two species. The closest homologues to B. colombiensis venom proteins appeared to be toxins from B. asper. A rough estimation of the similarity between the venoms of B. colombiensis and B. asper indicated that these species share approximately 65-70% of their venom proteomes. The close kinship of B. colombiensis and B. asper points at the ancestor of B. colombiensis as the founding Central American B. asper ancestor. This finding may be relevant for reconstructing the natural history and cladogenesis of Bothrops. Further, the virtually indistinguishable immunological crossreactivity of a Venezuelan ABC antiserum (raised against a mixture of B. colombiensis and Crotalus durissus cumanensis venoms) and the Costa Rican ICP polyvalent antivenom (generated against a mixture of B. asper, Crotalus simus, and Lachesis stenophrys venoms) towards the venoms of B. colombiensis and B. asper, supports this view and suggests the possibility of indistinctly using these antivenoms for the management of snakebites by any of these Bothrops species. However, our analyses also evidenced the limited recognition capability or avidity of these antivenoms towards a number of B. colombiensis and B. asper venom components, most notably medium-size disintegrins, bradykinin-potentiating peptides, PLA(2) proteins, and PI Zn(2+)-metalloproteinases.

Authors+Show Affiliations

Instituto de Biomedicina de Valencia, C.S.I.C., 46010 Valencia, Spain. jcalvete@ibv.csic.esNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19457355

Citation

Calvete, Juan J., et al. "Snake Venomics and Antivenomics of Bothrops Colombiensis, a Medically Important Pitviper of the Bothrops Atrox-asper Complex Endemic to Venezuela: Contributing to Its Taxonomy and Snakebite Management." Journal of Proteomics, vol. 72, no. 2, 2009, pp. 227-40.
Calvete JJ, Borges A, Segura A, et al. Snake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite management. J Proteomics. 2009;72(2):227-40.
Calvete, J. J., Borges, A., Segura, A., Flores-Díaz, M., Alape-Girón, A., Gutiérrez, J. M., Diez, N., De Sousa, L., Kiriakos, D., Sánchez, E., Faks, J. G., Escolano, J., & Sanz, L. (2009). Snake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite management. Journal of Proteomics, 72(2), 227-40. https://doi.org/10.1016/j.jprot.2009.01.005
Calvete JJ, et al. Snake Venomics and Antivenomics of Bothrops Colombiensis, a Medically Important Pitviper of the Bothrops Atrox-asper Complex Endemic to Venezuela: Contributing to Its Taxonomy and Snakebite Management. J Proteomics. 2009 Mar 6;72(2):227-40. PubMed PMID: 19457355.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Snake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite management. AU - Calvete,Juan J, AU - Borges,Adolfo, AU - Segura,Alvaro, AU - Flores-Díaz,Marietta, AU - Alape-Girón,Alberto, AU - Gutiérrez,José María, AU - Diez,Nardy, AU - De Sousa,Leonardo, AU - Kiriakos,Demetrio, AU - Sánchez,Eladio, AU - Faks,José G, AU - Escolano,José, AU - Sanz,Libia, Y1 - 2009/01/16/ PY - 2008/12/23/received PY - 2009/01/01/revised PY - 2009/01/07/accepted PY - 2009/5/22/entrez PY - 2009/5/22/pubmed PY - 2009/7/10/medline SP - 227 EP - 40 JF - Journal of proteomics JO - J Proteomics VL - 72 IS - 2 N2 - The taxonomic status of the medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela, which has been classified as Bothrops colombiensis, remains incertae cedis. To help resolving this question, the venom proteome of B. colombiensis was characterized by reverse-phase HPLC fractionation followed by analysis of each chromatographic fraction by SDS-PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass spectrometry of tryptic peptides. The venom contained proteins belonging to 8 types of families. PI Zn(2+)-metalloproteinases and K49 PLA(2) molecules comprise over 65% of the venom proteins. Other venom protein families comprised PIII Zn(2+)-metalloproteinases (11.3%), D49 PLA(2)s (10.2%), l-amino acid oxidase (5.7%), the medium-sized disintegrin colombistatin (5.6%), serine proteinases (1%), bradykinin-potentiating peptides (0.8%), a DC-fragment (0.5%), and a CRISP protein (0.1%). A comparison of the venom proteomes of B. colombiensis and B. atrox did not support the suggested synonymy between these two species. The closest homologues to B. colombiensis venom proteins appeared to be toxins from B. asper. A rough estimation of the similarity between the venoms of B. colombiensis and B. asper indicated that these species share approximately 65-70% of their venom proteomes. The close kinship of B. colombiensis and B. asper points at the ancestor of B. colombiensis as the founding Central American B. asper ancestor. This finding may be relevant for reconstructing the natural history and cladogenesis of Bothrops. Further, the virtually indistinguishable immunological crossreactivity of a Venezuelan ABC antiserum (raised against a mixture of B. colombiensis and Crotalus durissus cumanensis venoms) and the Costa Rican ICP polyvalent antivenom (generated against a mixture of B. asper, Crotalus simus, and Lachesis stenophrys venoms) towards the venoms of B. colombiensis and B. asper, supports this view and suggests the possibility of indistinctly using these antivenoms for the management of snakebites by any of these Bothrops species. However, our analyses also evidenced the limited recognition capability or avidity of these antivenoms towards a number of B. colombiensis and B. asper venom components, most notably medium-size disintegrins, bradykinin-potentiating peptides, PLA(2) proteins, and PI Zn(2+)-metalloproteinases. SN - 1874-3919 UR - https://www.unboundmedicine.com/medline/citation/19457355/Snake_venomics_and_antivenomics_of_Bothrops_colombiensis_a_medically_important_pitviper_of_the_Bothrops_atrox_asper_complex_endemic_to_Venezuela:_Contributing_to_its_taxonomy_and_snakebite_management_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1874-3919(09)00013-X DB - PRIME DP - Unbound Medicine ER -