Dataset Information

Venomics across the Bothrops neuwiedi species complex reveals a P-III SVMP/K49-PLA2 dichotomy and a remarkable paraspecific neutralization of the Brazilian pentabothropic antivenom

ABSTRACT: Snakes of the Bothrops neuwiedi complex have a widespread distribution, and represent medically important species in Brazil. Here, we report a compositional and functional profiles of the venom of seven species of the B. neuwiedi group: B. mattogrossensis, B. pauloensis, B. pubescens, B. diporus, B. neuwiedi, B. marmoratus and B. erythromelas. The toxin composition of individual and pooled venoms showed remarkable inter- and intraspecific variability of the relative abundance of toxins (evidenced by SDS-PAGE and RP-HPLC) and enzymatic activities (proteolytic, PLA2 and thrombin-like activities). In vivo analyses showed that B. erythromelas is the most haemorrhagic venom, B. diporus was the most lethal and B. pubescens venom showed the highest myotoxic activity. Histopathological analysis showed that the venom of the seven species caused edema, haemorrhage, inflammatory infiltrate and necrosis of muscle fibers. In line with large research evidence on the paraspecificity of various commercial antivenoms generated in Latin America for the treatment of human bothropic envenomings, the pentabothropic antivenom produced by Instituto Butantan showed a high profile of immunoreactivity and lethality neutralization capability towards the venoms of the seven species of the B. neuwiedi clade. Interpreted through the prism of Evolution, our data revealed a PIII-SVMP/K49-PLA2 compositional dichotomy and a remarkable conservation of immunological crossreactivity across congeneric venoms throughout the 12-16 million years of Bothrops phylogeny.

INSTRUMENT(S):

ORGANISM(S): Bothrops Mattogrossensis

TISSUE(S): Venom

SUBMITTER: Jordi Tena-Garces

LAB HEAD: Juan José Calvete Chornet

PROVIDER: PXD066646 | Pride | 2026-02-23

REPOSITORIES: Pride

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Venomics across the Bothrops neuwiedi Species Complex Revealed a P-III Snake Venom Metalloproteases/K49-PLA2 Dichotomy and a Remarkable Paraspecific Neutralization of the Brazilian Pentabothropic Antivenom.

Galizio Nathália da Costa NDC Serino-Silva Caroline C Fabri Bittencourt Rodrigues Caroline C Stuginski Daniel Rodrigues DR Rocha Marisa Maria Teixeira da MMTD Serapicos Eliana de Oliveira EO Barbarini Cibele Cintia CC Oliveira Roberto Baptista de RB Sant'Anna Sávio Stefanini SS Grego Kathleen Fernandes KF Sanz Libia L Tena-Garcés Jordi J de Roodt Adolfo R AR Calvete Juan J JJ Tanaka-Azevedo Anita Mitico AM de Morais-Zani Karen K

Journal of proteome research 20260122 2

Snakes of the Bothrops neuwiedi complex are widely distributed and represent medically important species in Brazil. Here, we report compositional and functional profiles of the venom of seven species of Bothrops neuwiedi group: Bothrops mattogrossensis, Bothrops pauloensis, Bothrops pubescens, Bothrops diporus, Bothrops neuwiedi, Bothrops marmoratus, and Bothrops erythromelas. Toxin composition of individual and pooled venoms showed ...[more]

PMID: 41570121

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Project description:Bothrops moojeni has a wide distribution in Brazil and represents a serious medical concern at some localities. Previous works reported that the manifestations of snakebites caused by B. moojeni juveniles were mainly related to coagulation, while those caused by adults had more prominent local damage. In this work, we aimed to analyze the venoms of B. moojeni at different life stages to better understand how the venom shifts along the ontogeny. Snakes were grouped by age and sex, and venom pools were formed accordingly. Compositional analyses by one-dimensional electrophoresis (1-DE), chromatography and mass spectrometry revealed that ontogenetic changes may be mostly related to phospholipase A2 (PLA2) and metalloproteases. Regarding the functional aspect of the venoms, in vitro assays of proteolytic, L-amino acid oxidase, PLA2 and coagulant activities were assayed, but only the first and the last showed age-related changes, with the venom of younger snakes displaying lower proteolytic and higher coagulant activities up to 1 year-old; from 2 years-old onward, the venoms presented the opposite relation. The venoms of 3 years-old snakes were exceptions to the compositional and functional pattern of adults. Sex-related differences were observed at specific groups and not related to age. In vivo experiments (median lethal dose and hemorrhagic activity) were statistically similar between neonates and adults, but observation of the time each venom took to kill the mice revealed that the adult one seemed to act faster than the venoms of the neonates. All venoms were mostly recognized by the antibothropic serum and displayed similar profiles to 1-DE in western blotting. In conclusion, the venoms showed ontogenetic shift in composition and activities. Furthermore, this change occurred from 1 to 2 years-old, and interestingly the 3 years-old pools had particular characteristics, which highlight the importance of extending the studies to better understand venom variability.

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.

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:Background The phenotypic polymorphism in rattlesnake venoms has been thoroughly documented, showing a dichotomy between haemorrhagic (Type I) and neurotoxic (Type II) venoms. In South America, the Type II phenotype is predominant; however, evidence exists of Type I haemorrhagic venoms in C. d. ruruima, raising questions about the efficacy of the Crotalus antivenom prepared for the Type II phenotype in treating Crotalus Type I snakebite patients, for whom the administration of Bothrops-Crotalus antivenom has been proposed. Methodology/Principal Findings This study characterises the dichotomy of C. d. ruruima venom based on the structure of isoforms differentially expressed in Type I and Type II venoms, the biological activities of each phenotype, and the implications for the clinical management of snakebites in Northern Brazil. Four toxins were differentially expressed in Type I and Type II venoms: two PIII-class SVMPs, which were highly expressed in Type I venoms and associated with proteolytic and haemorrhagic activity, and two PLA2s, corresponding to Crotoxin A and B chains, identified in Type II venoms and associated with increased phospholipase A2, myotoxic activities, and heightened lethality. The structure of Crotoxin chains was well conserved compared to C. d. terrificus crotoxin. However, compared to Bothropasin, the SVMP sequences exhibited several substitutions in functional and immunoreactive regions, resulting in low haemorrhagic activity and slight reactivity/neutralisation by Bothrops antivenom. In opposition, Crotalus antivenom reacted with high antibody titres and neutralised all activities of both venom subtypes, except the low haemorrhagic activity induced by Type I venoms. Conclusions/Significance The efficacy of Bothrops antivenom in incidents involving snakes of the Type I phenotype remains uncertain, and we advocate for an urgent prospective study in Roraima to assess the outcomes and benefits for patients receiving either Bothrops-Crotalus or solely Crotalus antivenoms following rattlesnake bites. Meanwhile, administering Bothrops-Crotalus antivenom could be warranted. However, it is crucial to remain aware of the issues of injecting heterologous Bothrops antibodies with limited efficacy in treating Crotalus snakebite patients.

			Action	DRS
	Bmt_11_CID.pkl	Other
	Bmt_13_CID.pkl	Other
	Bmt_18a_CID.pkl	Other
	Bmt_18b_CID.pkl	Other
	Bmt_19a_CID.pkl	Other

Dataset Information

Venomics across the Bothrops neuwiedi species complex reveals a P-III SVMP/K49-PLA2 dichotomy and a remarkable paraspecific neutralization of the Brazilian pentabothropic antivenom

Dataset's files

Publications

Venomics across the <i>Bothrops neuwiedi</i> Species Complex Revealed a P-III Snake Venom Metalloproteases/K49-PLA<sub>2</sub> Dichotomy and a Remarkable Paraspecific Neutralization of the Brazilian Pentabothropic Antivenom.

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Dataset Information

Venomics across the Bothrops neuwiedi species complex reveals a P-III SVMP/K49-PLA2 dichotomy and a remarkable paraspecific neutralization of the Brazilian pentabothropic antivenom

Dataset's files

Publications

Venomics across the &lt;i&gt;Bothrops neuwiedi&lt;/i&gt; Species Complex Revealed a P-III Snake Venom Metalloproteases/K49-PLA&lt;sub&gt;2&lt;/sub&gt; Dichotomy and a Remarkable Paraspecific Neutralization of the Brazilian Pentabothropic Antivenom.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Venomics across the <i>Bothrops neuwiedi</i> Species Complex Revealed a P-III Snake Venom Metalloproteases/K49-PLA<sub>2</sub> Dichotomy and a Remarkable Paraspecific Neutralization of the Brazilian Pentabothropic Antivenom.