N-glycome profiling of Bothrops jararaca newborn and adult venoms

Zelanis, André; Serrano, Solange M.T.; Reinhold, Vernon N.

doi:10.1016/j.jprot.2011.09.017

Cited by 33 publications

(27 citation statements)

References 32 publications

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“…Nevertheless, N-glycan composition studies of isolated toxins and venoms from Elapidae and Viperidae families indicate significant variability (33)(34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44)(45)(46). On the other hand, we have shown that the Bothrops jararaca N-glycan compositions from newborn and adult venoms are similar suggesting that differences in utilization might explain the variable glycosylation levels that were indicated by differential electrophoretic profiles previously reported for B. jararaca newborn and adult venoms (47).…”

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confidence: 48%

“…Feeding habits have long been associated to the variability in snake venoms and, in this context, toxin microheterogeneities such as N-linked glycans may be regarded as functional signatures of snake venom variability that would allow distinct species to deal with different prey types. This fine-tuning mechanism is both (1) parsimonial, as changing the glycan composition or N-glycosylation site occupancy helps to generate distinct glycoforms and (2) effective, as structural changes may result in new biological targets toward different prey types (47). However, a study on the characterization of the venom gland proteome of B. jararaca showed that glycosylation-related proteins represented a small fraction (17%) of all proteins involved with PTMs that were detected by mass spectrometry in the tissue.…”

Section: Discussionmentioning

confidence: 99%

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Structures of N-Glycans of Bothrops Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes

Andrade-Silva¹,

Ashline

Tran

et al. 2018

Molecular & Cellular Proteomics

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The complexity of snake venoms has long been investigated to explore a myriad of biologically active proteins and peptides that are used for immobilizing or killing prey, and are responsible for the pathological effects observed on envenomation. Glycosylation is the main post-translational modification (PTM) of viperid venoms but currently there is little understanding of how protein glycosylation impacts the variation of venom proteomes. We have previously reported that venom glycoproteomes contain a core of components that markedly define their composition and parallel their phylogenetic classification. Here we extend those observations to eight species evaluating the N-glycomes by LC-MS as assigned cartoon structures and detailing those structures separately as methylated analogs using ion-trap mass spectrometry (MS). Following ion disassembly through multiple steps provided sequence and linkage isomeric details that characterized 52 unique compositions in venoms. These occurred as 60 structures, of which 26 were identified in the venoms of the Jararaca Complex (, , and), 20 in ,, and venoms, and 22 in venom. Further, quantitative analysis of these N-glycans showed variable relative abundances in the venoms. For the first time a comprehensive set of N-glycan structures present in snake venoms are defined. Despite the fact that glycosylation is not template-defined, the N-glycomes of these venoms mirror the phylogeny cladograms of South American bothropoid snakes reported in studies on morphological, molecular data and feeding habits, exhibiting distinct molecular signatures for each venom. Considering the complexity of N-glycan moieties generally found in glycoproteins, characterized by different degrees of branching, isomer structures, and variable abundances, our findings point to these factors as another level of complexity in venoms, features that could dramatically contribute to their distinct biological activities.

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confidence: 48%

Section: Discussionmentioning

confidence: 99%

Structures of N-Glycans of Bothrops Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes

Andrade-Silva¹,

Ashline

Tran

et al. 2018

Molecular & Cellular Proteomics

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“…While D. typus venom is dominated by P-III SVMP (Figure 3.3), T. mossambicanus has a higher percentage of smaller toxins such as PLA2 and CRiSP than D. typus (Figure 3.1). The SVMP of both venoms were shown for the first time to be heavily glycosylated ( Figure 3.4), as has been previously shown for pit viper venoms such as Bothrops species (Andrade-Silva et al, 2016;Oliveira et al, 2010;Zelanis et al, 2012;Zelanis et al, 2010). Despite the fact that T. mossambicanus venom contains proportionally less procoagulant SVMPs than D. typus, T. mossambicanus is much more powerfully procoagulant (Debono et al, 2017a), due to stronger prothrombin activation compared to Dispholidus typus ( Figure 3.5).…”

Section: Discussionsupporting

confidence: 66%

A blood bond: evolutionary, pathophysiological and biodiscovery implications of coagulotoxic snake venoms

Debono¹

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Snakebite is a massive global burden and is a neglected area of tropical diseases. Snake venom neurotoxins have been the subject of intense research efforts, albeit significantly less is known about coagulotoxins. Venoms can deleteriously affect any physiological system reachable by the bloodstream, including being able to directly interfere with the coagulation cascade. Such coagulopathic toxins may be either anticoagulant or procoagulant and snake venoms are unique in their use of procoagulant toxins for predatory purposes. Our limited knowledge into the mechanisms of action of snake venom hinders our understanding of the clinical pathologies and also restricts our use of these powerful natural products as lead compounds in drug design and development. Two snake families which exhibit coagulant properties and lead to a range of clinical pathologies are vipers, Viperidae, and non-front-fanged snakes, Colubridae. The primary focus of this thesis was to investigate and compare the coagulotoxicity effects and mechanisms of various species of known venomous snakes that effect coagulation. Species chosen for this investigation have had limited previous research conducted, thus a knowledge gap in the literature remains. These coagulant properties were investigated through a multi-disciplinary approach, highlighting key results from both families.Data chapters 2 and 3 explore venom from the boomslang (Dispholidus typus) and the twig snakes (Thelotornis species) -iconic African snakes belonging to the family Colubridae. Both species produce strikingly similar lethal procoagulant pathologies. Despite these similarities, antivenom is only produced for treating bites by D. typus, and the mechanisms of action of both venoms have been understudied. We found that T. mossambicanus produced a significantly stronger coagulation response compared to D. typus, governed by strong prothrombin activation through PIII-SVMPs.Despite similarities in symptoms and clinical manifestations, venom composition differs widely between the two species, recovered from a combined approach of venomics and transcriptomics. The neutralising capability of the available boomslang antivenom was also investigated on both species, with it being 11.3 times more effective upon D. typus venom than T. mossambicanus. Envenomation by Crotalinae such as Asian pit vipers can induce multiple clinical complications resulting from coagulopathic and neuropathic effects. Data chapters 4 -8 investigate the Asian Pit Viper clade. While intense research has been undertaken for some species, such as Calloselasma rhodostoma, functional coagulopathic effects have been neglected. As these species' venoms affect the blood coagulation cascade and are known to produce haemorrhagic shock in envenomed patients, we investigated their effects upon coagulation using venoms of 33 species from the Asian pit viper clade including Azemiops, Calloselasma, Deinagkistrodon, Gloydius, Hypnale, Protobothrops, Trimeresurus and Tropidolaemus. Fibrinogen was the main coagulation target among th...

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“…Some components of snake venom are known to possess glycosylation; however, little is known about the structure of the carbohydrates present in these proteins [55]. …”

Section: Resultsmentioning

confidence: 99%

Biochemical and Functional Characterization ofParawixia bistriataSpider Venom with Potential Proteolytic and Larvicidal Activities

Gimenez

Coutinho-Neto

Kayano

et al. 2014

BioMed Research International

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Toxins purified from the venom of spiders have high potential to be studied pharmacologically and biochemically. These biomolecules may have biotechnological and therapeutic applications. This study aimed to evaluate the protein content of Parawixia bistriata venom and functionally characterize its proteins that have potential for biotechnological applications. The crude venom showed no phospholipase, hemorrhagic, or anti-Leishmania activities attesting to low genotoxicity and discrete antifungal activity for C. albicans. However the following activities were observed: anticoagulation, edema, myotoxicity and proteolysis on casein, azo-collagen, and fibrinogen. The chromatographic and electrophoretic profiles of the proteins revealed a predominance of acidic, neutral, and polar proteins, highlighting the presence of proteins with high molecular masses. Five fractions were collected using cation exchange chromatography, with the P4 fraction standing out as that of the highest purity. All fractions showed proteolytic activity. The crude venom and fractions P1, P2, and P3 showed larvicidal effects on A. aegypti. Fraction P4 showed the presence of a possible metalloprotease (60 kDa) that has high proteolytic activity on azo-collagen and was inhibited by EDTA. The results presented in this study demonstrate the presence of proteins in the venom of P. bistriata with potential for biotechnological applications.

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N-glycome profiling of Bothrops jararaca newborn and adult venoms

Cited by 33 publications

References 32 publications

Structures of N-Glycans of Bothrops Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes

Structures of N-Glycans of Bothrops Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes

A blood bond: evolutionary, pathophysiological and biodiscovery implications of coagulotoxic snake venoms

Biochemical and Functional Characterization ofParawixia bistriataSpider Venom with Potential Proteolytic and Larvicidal Activities

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