Some aspects of the venom proteome of the Colubridae snake <i>Philodryas olfersii</i> revealed from a Duvernoy's (venom) gland transcriptome

Ching, Ana Tung Ching; Rocha, Marisa Maria Teixeira da; Leme, Adriana Franco Paes; Pimenta, Daniel C.; Furtado, Maria de Fátima D.; Serrano, Solange M.T.; Ho, Paulo Lee; Junqueira-de-Azevedo, Inácio L.M.

doi:10.1016/j.febslet.2006.07.010

Cited by 109 publications

(102 citation statements)

References 28 publications

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“…expected from published data, B. arietans venom protein contains antigenic epitopes recognized by antibodies generated by non-Viperidae snake venoms (Junqueirade-Azevedo and Ho, 2002;Guo et al, 2007;Ching et al, 2006). In fact, in this study, we experimentally demonstrated that the isolated 50-kDa protein was recognized by antibodies present in horse polyclonal F(ab´) 2 or in chicken IgY anti-Bitis arietans, anti-Bitis spp., anti-Naja spp., anti-Lachesis muta, anti-Bothrops spp., and antiCrotalus spp.…”

Section: Discussionsupporting

confidence: 61%

“…Previous studies indicate that SVMPs and ADAMs are involved in hemorrhage, edema, hypotension, inflammation and necrosis induced by snake venoms (Gutiérrez and Rucovaldo, 2000). Although Viperidae snake venoms are rich in SVMPs, these enzymes have also been observed in certain Elapidae and Colubridae venoms (Junqueira-de-Azevedo and Ho, 2002;Guo et al, 2007;Ching et al 2006). SVMPs act by cleaving proteins on the vascular basement membrane and surrounding connective tissues as well as by altering platelet structure and function.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Souza¹,

Magnoli²,

Silva³

2015

Afr. J. Biotechnol.

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Better characterization of individual snake venom toxins is useful for analyzing the association of their toxic domains and relevant antigenic epitopes. Here we analyzed the Bitis arietans hemorrhagicinducing toxin present in a representative venom sample. Among the 1´ to 5´ protein peaks isolated using a Sephacryl S 100 HR chromatography column, hemorrhagic activity was expressed by all according to the following intensity, P´5 > P´3 > P´2 >, P´4. The proteins were recognized and measured with antibodies present in polyvalent horse F(ab)´2 anti-B. arietans, Bitis spp., Lachesis muta, B. atrox, Bothrops spp., Crotalus spp., and Naja spp. or in IgY anti-B. arietans and anti-Bitis spp. using enzymelinked immunosorbent assays and western blotting. In addition, in an in vitro-in vivo assay these antivenoms were able to block hemorrhagic-inducing activity. The evident cross-reactivity expressed by different specific anti-venoms indicates that metalloproteinases induce an immunological signature indicating the presence of similar antigenic epitopes for several snake venoms.

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Section: Discussionsupporting

confidence: 61%

Section: Introductionmentioning

confidence: 99%

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Souza¹,

Magnoli²,

Silva³

2015

Afr. J. Biotechnol.

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“…Consistent with the lack of atrial natriuretic peptide in the reptile physiology (29), the lizard venom types were nested within the BNP clade. In contrast, as reported previously (30), the snake forms were all nested within the CNP clade (Fig. 7).…”

Section: Resultscontrasting

confidence: 52%

Functional and Structural Diversification of the Anguimorpha Lizard Venom System

Fry

Winter

Norman

et al. 2010

Molecular & Cellular Proteomics

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Because of significant differences in anatomy of the venom delivery system and distant phylogenetic relatedness, it had been long assumed that the venom systems of snakes and helodermatid lizards were independently evolved (1-3). However, both lineages were recently revealed to be members of a clade (Toxicofera) that also included several lineages of other lizards recently shown to be venomous (4, 5). In contrast to the hypothesis of independent origins, this new perspective revealed that lizard and snake venom systems are homologous but highly differentiated descendants of an early evolved venom system in squamates. The basal condition was incipient glands on both the mandibular and maxillary regions with snakes favoring the maxillary venom glands and secondarily losing the mandibular venom glands. However, the anguimorph lizards (anguids, helodermatids, and varanids) did the reverse, resulting in the modern condition seen today.The lizard venom delivery system is less sophisticated than the high pressure injection mechanism of the front fanged advanced snakes, and the vast majority of the species pose trivial direct medical risks to human (with the exception of helodermatids and large varanids such as Varanus komodoensis). However, the effects of envenomation from mediFrom the

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“…13). The homomeric and the heterodimeric lectin forms had been considered previously to be the result of two separate toxin recruitment events (3) or the result of a single recruitment event (18). However, reconstructing the evolutionary history had been hampered by the scarcity of homomeric sequences.…”

Section: Evolution Of An Arsenalmentioning

confidence: 99%

Evolution of an Arsenal

Fry

Scheib²,

Weerd³

et al. 2008

Molecular & Cellular Proteomics

308

145

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Venom is a key innovation underlying the evolution of advanced snakes (Caenophidia). Despite this, very little is known about venom system structural diversification, toxin recruitment event timings, or toxin molecular evolution. A multidisciplinary approach was used to examine the diversification of the venom system and associated toxins across the full range of the ϳ100 million-year-old advanced snake clade with a particular emphasis upon families that have not secondarily evolved a front-fanged venom system (ϳ80% of the 2500 species). Analysis of cDNA libraries revealed complex venom transcriptomes containing multiple toxin types including three finger toxins, cobra venom factor, cysteine-rich secretory protein, hyaluronidase, kallikrein, kunitz, lectin, matrix metalloprotease, phospholipase A 2 , snake venom metalloprotease/a disintegrin and metalloprotease, and waprin. High levels of sequence diversity were observed, including mutations in structural and functional residues, changes in cysteine spacing, and major deletions/truncations. Morphological analysis comprising gross dissection, histology, and magnetic resonance imaging also demonstrated extensive modification of the venom system architecture in nonfront-fanged snakes in contrast to the conserved structure of the venom system within the independently evolved front-fanged elapid or viperid snakes. Further, a reduction in the size and complexity of the venom system was observed in species in which constriction has been secondarily evolved as the preferred method of prey capture or dietary preference has switched from live prey to eggs or to slugs/snails. Investigation of the timing of toxin recruitment events across the entire advanced snake radiation indicates that the evolution of advanced venom systems in three front-fanged lineages is associated with recruitment of new toxin types or explosive diversification of existing toxin types. These results support the role of venom as a key evolutionary innovation in the diversification of advanced snakes and identify a potential role for non-front-fanged venom toxins as a rich source for lead compounds for drug design and development.

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Some aspects of the venom proteome of the Colubridae snake Philodryas olfersii revealed from a Duvernoy's (venom) gland transcriptome

Cited by 109 publications

References 28 publications

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Characterization of a hemorrhage-inducing component present in Bitis arietans venom

Functional and Structural Diversification of the Anguimorpha Lizard Venom System

Evolution of an Arsenal

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