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Venomics of the Duvernoy's gland secretion of the false coral snake Rhinobothryum bovallii (Andersson, 1916) and assessment of venom lethality towards synapsid and diapsid animal models.
J Proteomics. 2020 Aug 15; 225:103882.JP

Abstract

The Duvernoy's gland secretory proteome of the false coral snake Rhinobothryum bovallii (Costa Rica), unveiled applying bottom-up venomics, comprises a handful of toxins belonging to only three protein families, three-finger toxin (3FTx), cysteine-rich secretory protein (CRISP), and snake venom metalloprotease (PIII-SVMP). Except for small differences in the relative abundance of the PIII-SVMPs, which may be due to individual variability, no evidence of geographic variability or ontogenetic changes was found among the venom proteomes of the juvenile and adult R. bovallii snakes sampled. Major monomeric (86.5%mol) and minor dimeric (2.8%mol) 3FTxs dominate the toxin arsenal of the Costa Rican false coral snake. The remaining 10.7% of the venom proteome comprises CRISP (8.2%) and PIII-SVMP (2.4%) molecules. In vivo lethality assays showed that R. bovallii produces venom that is non-toxic towards mammalian prey, and which exerts a different toxic effect on domestic chicken chicks and baby green iguana. Toxicovenomic analysis of R. bovallii venom in the iguana model identified two 3FTx RP-HPLC fractions that faithfully mimicked the irreversible immobilizing effect of the whole venom. BIOLOGICAL

SIGNIFICANCE:

With more than 2200 species in family Colubridae (sensu lato), rear-fanged snakes comprise approximately two-thirds of the extant species of advanced snakes. Snakebites from venomous snakes that are of medical concern are predominantly from front-fanged snakes of families Viperidae and Elapidae. On the other hand, rear-fanged snakes have been conventionally considered non-venomous, and thus their venoms have remained a largely untapped area of venomics. However, increasing documentation of life-threadening, even fatal, envenomings from rear-fanged snakes has sparked interest in their venoms. Appying bottom-up venomics we have revealed that the Duvernoy's gland secretory proteome of R. bovallii comprises a handful of toxins belonging to only three protein families, with slow-acting three-finger toxins (3FTx) that are non-toxic towards mammalian prey and show preference towards diapsid taxa representing the dominant structural and functional proteins. Our work documents for the first time 3FTxs exerting different effect in an avian model than in a reptile model. Besides, the 3FTx fractions that faithfully mimicked the irreversible iguana-immobilizing effect of the whole venom were identified through toxicovenomic analysis of R. bovallii venom on Iguana iguana. Our work underscores the importance of using biologically-relevant animal toxicity models for investigating the biological roles of venoms in an evolutionary-ecological context.

Authors+Show Affiliations

Evolutionary and Translational Venomics Lab, Instituto de Biomedicina de Valencia, CSIC, Valencia, Spain. Electronic address: jcalvete@ibv.csic.es.Laboratorio de Investigación en Animales Peligrosos (LIAP), Costa Rica; Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 11501, Costa Rica. Electronic address: fbonillamurillo@gmail.com.Laboratorio de Investigación en Animales Peligrosos (LIAP), Costa Rica; Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 11501, Costa Rica.Evolutionary and Translational Venomics Lab, Instituto de Biomedicina de Valencia, CSIC, Valencia, Spain. Electronic address: Libia.Sanz@ibv.csic.es.Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 11501, Costa Rica. Electronic address: Bruno.Lomonte@ucr.ac.cr.Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 11501, Costa Rica; Escuela de Biología, Universidad de Costa Rica, San José, Costa Rica. Electronic address: msasamarin@gmail.com.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32598980

Citation

Calvete, Juan J., et al. "Venomics of the Duvernoy's Gland Secretion of the False Coral Snake Rhinobothryum Bovallii (Andersson, 1916) and Assessment of Venom Lethality Towards Synapsid and Diapsid Animal Models." Journal of Proteomics, vol. 225, 2020, p. 103882.
Calvete JJ, Bonilla F, Granados-Martínez S, et al. Venomics of the Duvernoy's gland secretion of the false coral snake Rhinobothryum bovallii (Andersson, 1916) and assessment of venom lethality towards synapsid and diapsid animal models. J Proteomics. 2020;225:103882.
Calvete, J. J., Bonilla, F., Granados-Martínez, S., Sanz, L., Lomonte, B., & Sasa, M. (2020). Venomics of the Duvernoy's gland secretion of the false coral snake Rhinobothryum bovallii (Andersson, 1916) and assessment of venom lethality towards synapsid and diapsid animal models. Journal of Proteomics, 225, 103882. https://doi.org/10.1016/j.jprot.2020.103882
Calvete JJ, et al. Venomics of the Duvernoy's Gland Secretion of the False Coral Snake Rhinobothryum Bovallii (Andersson, 1916) and Assessment of Venom Lethality Towards Synapsid and Diapsid Animal Models. J Proteomics. 2020 Aug 15;225:103882. PubMed PMID: 32598980.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Venomics of the Duvernoy's gland secretion of the false coral snake Rhinobothryum bovallii (Andersson, 1916) and assessment of venom lethality towards synapsid and diapsid animal models. AU - Calvete,Juan J, AU - Bonilla,Fabián, AU - Granados-Martínez,Sofía, AU - Sanz,Libia, AU - Lomonte,Bruno, AU - Sasa,Mahmood, Y1 - 2020/06/27/ PY - 2020/04/12/received PY - 2020/06/16/revised PY - 2020/06/16/accepted PY - 2020/7/1/pubmed PY - 2020/7/1/medline PY - 2020/6/30/entrez KW - Colubridae 3FTx KW - Diapsid-specific venom toxin KW - Duvernoy's gland secretion KW - Rear-fanged snake KW - Rhinobothryum bovallii KW - Snake venomics KW - Toxicovenomics SP - 103882 EP - 103882 JF - Journal of proteomics JO - J Proteomics VL - 225 N2 - The Duvernoy's gland secretory proteome of the false coral snake Rhinobothryum bovallii (Costa Rica), unveiled applying bottom-up venomics, comprises a handful of toxins belonging to only three protein families, three-finger toxin (3FTx), cysteine-rich secretory protein (CRISP), and snake venom metalloprotease (PIII-SVMP). Except for small differences in the relative abundance of the PIII-SVMPs, which may be due to individual variability, no evidence of geographic variability or ontogenetic changes was found among the venom proteomes of the juvenile and adult R. bovallii snakes sampled. Major monomeric (86.5%mol) and minor dimeric (2.8%mol) 3FTxs dominate the toxin arsenal of the Costa Rican false coral snake. The remaining 10.7% of the venom proteome comprises CRISP (8.2%) and PIII-SVMP (2.4%) molecules. In vivo lethality assays showed that R. bovallii produces venom that is non-toxic towards mammalian prey, and which exerts a different toxic effect on domestic chicken chicks and baby green iguana. Toxicovenomic analysis of R. bovallii venom in the iguana model identified two 3FTx RP-HPLC fractions that faithfully mimicked the irreversible immobilizing effect of the whole venom. BIOLOGICAL SIGNIFICANCE: With more than 2200 species in family Colubridae (sensu lato), rear-fanged snakes comprise approximately two-thirds of the extant species of advanced snakes. Snakebites from venomous snakes that are of medical concern are predominantly from front-fanged snakes of families Viperidae and Elapidae. On the other hand, rear-fanged snakes have been conventionally considered non-venomous, and thus their venoms have remained a largely untapped area of venomics. However, increasing documentation of life-threadening, even fatal, envenomings from rear-fanged snakes has sparked interest in their venoms. Appying bottom-up venomics we have revealed that the Duvernoy's gland secretory proteome of R. bovallii comprises a handful of toxins belonging to only three protein families, with slow-acting three-finger toxins (3FTx) that are non-toxic towards mammalian prey and show preference towards diapsid taxa representing the dominant structural and functional proteins. Our work documents for the first time 3FTxs exerting different effect in an avian model than in a reptile model. Besides, the 3FTx fractions that faithfully mimicked the irreversible iguana-immobilizing effect of the whole venom were identified through toxicovenomic analysis of R. bovallii venom on Iguana iguana. Our work underscores the importance of using biologically-relevant animal toxicity models for investigating the biological roles of venoms in an evolutionary-ecological context. SN - 1876-7737 UR - https://www.unboundmedicine.com/medline/citation/32598980/Venomics_of_the_Duvernoy's_gland_secretion_of_the_false_coral_snake_Rhinobothryum_bovallii_(Andersson,_1916)_and_assessment_of_venom_lethality_towards_synapsid_and_diapsid_animal_models L2 - https://linkinghub.elsevier.com/retrieve/pii/S1874-3919(20)30250-5 DB - PRIME DP - Unbound Medicine ER -
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