Proteomic and functional profiling of the venom of Bothrops ayerbei from Cauca, Colombia, reveals striking interspecific variation with Bothrops asper venom

Mora-Obando, Diana; Guerrero-Vargas, Jimmy Alexander; Prieto-Sánchez, Rodrigo; Beltrán, José; Rucavado, Alexandra; Sasa, Mahmood; Gutiérrez, José Marı́a; Ayerbe, Santiago; Lomonte, Bruno

doi:10.1016/j.jprot.2013.11.005

Cited by 36 publications

(30 citation statements)

References 34 publications

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“…Shotgun mass spectrometry recovered proteins of known pitviper toxin types ( Table 1 ) in agreement with previous proteomic [ 10 , 11 , 13 , 14 , 30 , 32 , 83 , 84 , 92 ] and transcriptomic analyses [ 22 , 24 , 29 , 59 , 77 , 89 , 90 , 93 , 95 , 97 , 103 ].…”

Section: Resultssupporting

confidence: 86%

“…Despite the medical significance of pitviper envenomations in the New World [ 78 , 79 , 80 , 81 , 82 , 83 ], the majority of toxinological research published to date has been on North American members of the genus Crotalus [ 14 , 25 , 26 , 35 , 38 , 39 , 40 , 41 , 42 , 43 , 49 , 50 , 82 , 83 , 84 , 85 , 86 , 87 , 88 , 89 , 90 ], and the larger members of the genus Bothrops [ 10 , 91 , 92 , 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 , 101 , 102 , 103 , 104 ]. While investigations into Bothriechis , in particular B .…”

Section: Introductionmentioning

confidence: 99%

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Canopy Venom: Proteomic Comparison among New World Arboreal Pit-Viper Venoms

Debono

Cochran

Kuruppu

et al. 2016

Toxins

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Central and South American pitvipers, belonging to the genera Bothrops and Bothriechis, have independently evolved arboreal tendencies. Little is known regarding the composition and activity of their venoms. In order to close this knowledge gap, venom proteomics and toxin activity of species of Bothriechis, and Bothrops (including Bothriopsis) were investigated through established analytical methods. A combination of proteomics and bioactivity techniques was used to demonstrate a similar diversification of venom composition between large and small species within Bothriechis and Bothriopsis. Increasing our understanding of the evolution of complex venom cocktails may facilitate future biodiscoveries.

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Section: Resultssupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Canopy Venom: Proteomic Comparison among New World Arboreal Pit-Viper Venoms

Debono

Cochran

Kuruppu

et al. 2016

Toxins

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“…, 2009; Alape-Girón et al. , 2008), a comparison of their venom compositions, together with those of two other pitviper species distributed in Colombia, Bothrops ayerbei (Mora-Obando et al. , 2014) and Bothriechis schlegelii (Lomonte et al.…”

Section: Resultsmentioning

confidence: 99%

Snake venomics ofBothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia

Culma¹,

Pereañez²,

Rangel

et al. 2014

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Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panamá, 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 (93%), serine proteinases (5.4%), disintegrins (38%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (17%), 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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“…These changes in venom composition have been mostly correlated to the sexual maturation of the snakes. However, most of these studies used a fixed threshold value of SVL as a measure to determine if snakes are in the juvenile or adult stages [17,26,30,[55][56][57]. As shown here, this definition does not apply to B. jararacussu.…”

Section: Discussionmentioning

confidence: 99%

Size Matters: An Evaluation of the Molecular Basis of Ontogenetic Modifications in the Composition of Bothrops jararacussu Snake Venom

Freitas-de-Sousa

Nachtigall

Portes-Junior

et al. 2020

Toxins

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Ontogenetic changes in venom composition have been described in Bothrops snakes, but only a few studies have attempted to identify the targeted paralogues or the molecular mechanisms involved in modifications of gene expression during ontogeny. In this study, we decoded B. jararacussu venom gland transcripts from six specimens of varying sizes and analyzed the variability in the composition of independent venom proteomes from 19 individuals. We identified 125 distinct putative toxin transcripts, and of these, 73 were detected in venom proteomes and only 10 were involved in the ontogenetic changes. Ontogenetic variability was linearly related to snake size and did not correspond to the maturation of the reproductive stage. Changes in the transcriptome were highly predictive of changes in the venom proteome. The basic myotoxic phospholipases A2 (PLA2s) were the most abundant components in larger snakes, while in venoms from smaller snakes, PIII-class SVMPs were the major components. The snake venom metalloproteinases (SVMPs) identified corresponded to novel sequences and conferred higher pro-coagulant and hemorrhagic functions to the venom of small snakes. The mechanisms modulating venom variability are predominantly related to transcriptional events and may consist of an advantage of higher hematotoxicity and more efficient predatory function in the venom from small snakes.

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Proteomic and functional profiling of the venom of Bothrops ayerbei from Cauca, Colombia, reveals striking interspecific variation with Bothrops asper venom

Cited by 36 publications

References 34 publications

Canopy Venom: Proteomic Comparison among New World Arboreal Pit-Viper Venoms

Canopy Venom: Proteomic Comparison among New World Arboreal Pit-Viper Venoms

Snake venomics ofBothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia

Size Matters: An Evaluation of the Molecular Basis of Ontogenetic Modifications in the Composition of Bothrops jararacussu Snake Venom

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