Dataset Information

High-throughput proteomics of the 26 medically most important elapids and vipers from sub-Saharan Africa

ABSTRACT: Venomous snakes are important parts of the ecosystem, and their behavior and evolution have been shaped by their surrounding environments over the eons. This is reflected in their venoms, which are typically highly adapted for their biological niche, including their diet and defense mechanisms for deterring predators. Sub-Saharan Africa is rich in venomous snake species, of which many are dangerous to humans due to the high toxicity of their venoms and their ability to effectively deliver large amounts of venom into their victims via their bite. In this study, the venoms of 26 of sub-Saharan Africa’s medically most relevant elapid and viper species were subjected to parallelized toxicovenomics analysis. The analysis included venom proteomics and enables a robust comparison of venom profiles between species. Moreover, two new venom proteomes (N. anchietae and E. leucogaster) are presented here for the first time.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Naja Annulifera Naja Haje Naja Anchietae Naja Nubiae Echis Pyramidum Naja Melanoleuca Naja Ashei Naja Katiensis Dendroaspis Viridis Naja Senegalensis Dendroaspis Angusticeps (eastern Green Mamba) (naja Angusticeps) Cerastes Cerastes Naja Mossambica Naja Nivea Bitis Arietans Bitis Rhinoceros Echis Ocellatus Hemachatus Haemachatus Naja Nigricollis Naja Nigricincta Dendroaspis Jamesoni Bitis Gabonica Dendroaspis Polylepis Bitis Nasicornis Echis Leucogaster Naja Pallida

TISSUE(S): Venom

SUBMITTER: Carol O'Brien

LAB HEAD: Andreas H. Laustsen

PROVIDER: PXD036161 | Pride | 2022-10-17

REPOSITORIES: Pride

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			Action	DRS
	20220113_KMJ_MWN_15cm_70min_100ng_Carol_Batch2_10Nni.raw	Raw
	20220113_KMJ_MWN_15cm_70min_100ng_Carol_Batch2_11Nnv.raw	Raw
	20220113_KMJ_MWN_15cm_70min_100ng_Carol_Batch2_12Np.raw	Raw
	20220113_KMJ_MWN_15cm_70min_100ng_Carol_Batch2_13Ns.raw	Raw
	20220113_KMJ_MWN_15cm_70min_100ng_Carol_Batch2_14Nu.raw	Raw

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Project description:Snake venoms have evolved in a few families of Caenophidae, and their toxins have been fine-tuned over the evolutive process into highly effective biochemical weapons with a particular role as a trophic adaptation. However, there are many outstanding questions on how venom contributes to the success of venomous species and their adaptation to different environments. Here we analyze the venoms from sympatric and generalist specimens of B. hyoprora, B. taeniatus, B. b. smaragdinus, B. brazili, and B. atrox collected in the wild of Alto Juruá region at the Amazon Forest aiming to understand whether the venom composition could be a driver or influence the arboreal habitats of B. taeniatus and B. b. smaragdinus, or the successful dispersion of B. atrox across the Amazon Forest. Venom composition and the primary sequences of toxin isoforms were characterized by venom gland transcriptomics followed by proteomics. The venom composition of the five species conserved the same protein families present in venoms of Bothropoid snakes but with remarkable differences in the chromatographic profiles and in the relative amount of each toxin group: CTLs were the most abundant in the venoms of B. taeniatus (31.6%), B. b. smaragdinus (33.0%), and B. atrox (32.0%) and SVMPs and PLA2s dominated in venoms of B. hyoprora (23.7% and 20.2%) and B. brazili (20.2% and 20.4%). Some peculiarities were also observed: B. hyoprora venom was the least complex, conserving important isoforms shared with B. atrox venom; the presence of one cluster of SVSPs exclusive to B. brazili venom isoforms; and the presence of the K49-PLA2 homologs only in B. b. smaragdinus and particularly in B. brazili venoms. The SVMP, SVSP, and PLA2 enzyme activities were consistent with the abundance and type of isoforms present in the venoms. B. hyoprora, B. taeniatus, B. b. smaragdinus, and B. atrox venoms presented low lethality to small rodents, while B. brazili venom was the most lethal. Concluding, differences were evidenced between the venoms of B. taeniatus and B. b. smaragdinus arboreal species, while B. b. smaragdinus shared a venom with a similar composition to B. atrox venom, mostly terrestrial. Considering the role of venom toxicity in species' success for adaptation in different areas, B. atrox is the most adapted in the whole Amazonian territory and presented the least lethal venom, while the venom of B. brazili was the most lethal despite its small distribution in the same area. Therefore, our data suggest that the selection of venom composition may not influence the success or behavior of snake species. In this way, other biotic or abiotic factors influence their foraging status or their dispersal in different ecological niches.

Project description:Snake venoms are complex protein mixtures with different biological activities that can act in both their preys and human victims. Many of these proteins play a role in prey capture and in the digestive process of these animals. It is known that some snakes are resistant to the toxicity of their own venom by mechanisms not yet fully elucidated. However, it was observed in the Laboratory of Herpetology of Instituto Butantan that some Bothrops moojeni individuals injured by the same snake species showed mortalities caused by envenoming effects. This study analyzed the biochemical composition of 13 venom and plasma samples from Bothrops moojeni specimens to assess differences in their protein composition. Application of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed distinct venom protein profiles, but very homogeneous plasma profiles. Western Blotting (WB) was performed with plasma samples, which were submitted to incubation with the respective venom. Some individuals showed an immunorecognized band zone around 25 kDa, indicating interaction between the same individual plasma and venom proteins. Crossed-WB assay using non-self-plasma and venom showed that this variability is due to venom protein composition instead of plasma composition. These venoms presented higher caseinolytic, collagenolytic and coagulant activities than the venoms without these regions recognized by WB. Mass spectrometry analysis revealed that these individuals present, in addition to higher protein concentrations, other exclusive proteins in their composition. When these samples were tested in vivo, the results also showed higher lethality in these venoms, but lower hemorrhagic activity than in the venoms without these regions recognized by WB. In conclusion, some Bothrops moojeni specimens differ in venom composition, which may have implications in envenomation. Moreover, the high individual venom variability found in this species demonstrates the importance to work with individual analysis in studies involving intraspecific venom variability and venom evolution.

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High-throughput proteomics of the 26 medically most important elapids and vipers from sub-Saharan Africa

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