Proteomic and functional analyses of the venom of Porthidium lansbergii lansbergii (Lansberg's hognose viper) from the Atlantic Department of Colombia

Jiménez-Charris, Eliécer; Montealegre–Sánchez, Leonel; Solano–Redondo, Luis; Mora-Obando, Diana; Camacho, E.; Castro-Herrera, Fernando; Fierro–Pérez, Leonardo; Lomonte, Bruno

doi:10.1016/j.jprot.2014.11.016

Cited by 37 publications

(25 citation statements)

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“…Recent studies on the proteomic characterization of venoms are increasingly combining identification data with functional assays of particular components, to gain deeper insights from the medical and biological perspectives [57, 83–85]. The TS is conceptually identical to the ‘lethal neurotoxicity coefficient’ (LNC) defined as the ratio between the average LD 50 and the crotoxin + crotamine relative abundance (% of the total venom proteins) [50].…”

Section: Toxicovenomics: Unmasking the Villains Among The Crowdmentioning

confidence: 99%

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

Lomonte

Calvete

2017

J Venom Anim Toxins Incl Trop Dis

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129

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This work offers a general overview on the evolving strategies for the proteomic analysis of snake venoms, and discusses how these may be combined through diverse experimental approaches with the goal of achieving a more comprehensive knowledge on the compositional, toxic, and immunological characteristics of venoms. Some recent developments in this field are summarized, highlighting how strategies have evolved from the mere cataloguing of venom components (proteomics/venomics), to a broader exploration of their immunological (antivenomics) and functional (toxicovenomics) characteristics. Altogether, the combination of these complementary strategies is helping to build a wider, more integrative view of the life-threatening protein cocktails produced by venomous snakes, responsible for thousands of deaths every year.

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Section: Toxicovenomics: Unmasking the Villains Among The Crowdmentioning

confidence: 99%

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

Lomonte

Calvete

2017

J Venom Anim Toxins Incl Trop Dis

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129

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“…We also found a singleton (BC32, 0.3 % of total toxins) encoding a phosphodiesterase, which showed 81 % identity with a phosphodiesterase from Ovophis okinavensis . Several transcriptomic and proteomic studies reported the expression of these toxins in various snakes [ 24 , 65 , 84 – 88 ]. However, the function of these enzymes during envenomation remains unclear.…”

Section: Resultsmentioning

confidence: 99%

Gene expression profiling of the venom gland from the Venezuelan mapanare (Bothrops colombiensis) using expressed sequence tags (ESTs)

et al. 2016

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BackgroundBothrops colombiensis is a highly dangerous pit viper and responsible for over 70 % of snakebites in Venezuela. Although the composition in B. colombiensis venom has been identified using a proteome analysis, the venom gland transcriptome is currently lacking.ResultsWe constructed a cDNA library from the venom gland of B. colombiensis, and a set of 729 high quality expressed sequence tags (ESTs) was identified. A total number of 344 ESTs (47.2 % of total ESTs) was related to toxins. The most abundant toxin transcripts were metalloproteinases (37.5 %), phospholipases A2s (PLA2, 29.7 %), and serine proteinases (11.9 %). Minor toxin transcripts were linked to waprins (5.5 %), C-type lectins (4.1 %), ATPases (2.9 %), cysteine-rich secretory proteins (CRISP, 2.3 %), snake venom vascular endothelium growth factors (svVEGF, 2.3 %), L-amino acid oxidases (2 %), and other putative toxins (1.7 %). While 160 ESTs (22 % of total ESTs) coded for translation proteins, regulatory proteins, ribosomal proteins, elongation factors, release factors, metabolic proteins, and immune response proteins. Other proteins detected in the transcriptome (87 ESTs, 11.9 % of total ESTs) were undescribed proteins with unknown functions. The remaining 138 (18.9 %) cDNAs had no match with known GenBank accessions.ConclusionThis study represents the analysis of transcript expressions and provides a physical resource of unique genes for further study of gene function and the development of novel molecules for medical applications.Electronic supplementary materialThe online version of this article (doi:10.1186/s12867-016-0059-7) contains supplementary material, which is available to authorized users.

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“…Snake toxin genes are coded by gene families and produce gene isoforms through the process of duplications ( Casewell et al, 2013 ; Fry, 2005 ). Several studies on the venom-associated proteins from New World vipers have classified the venoms into four groups (type I–IV), based on the relative abundance of toxin families ( Calvete, 2013 ; Gibbs et al, 2013 ; Goncalves-Machado et al, 2016 ; Jimenez-Charris et al, 2015 ; Lomonte et al, 2014 ; Mora-Obando et al, 2014 ; Pla et al, 2017 ; Salazar-Valenzuela et al, 2014 ). The different groups are: snake venom metalloproteinase-predominant (type I), heterodimeric β -neurotoxic PLA2 –rich (type II), serine proteinases and PLA2 (type III) and type IV, which is similar to type III but with significant higher concentration of snake venom metalloproteinases ( Calvete, 2017 ).…”

Section: Discussionmentioning

confidence: 99%

Comparative analyses of putative toxin gene homologs from an Old World viper,Daboia russelii

Krishnan

Panda

2017

PeerJ

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Availability of snake genome sequences has opened up exciting areas of research on comparative genomics and gene diversity. One of the challenges in studying snake genomes is the acquisition of biological material from live animals, especially from the venomous ones, making the process cumbersome and time-consuming. Here, we report comparative sequence analyses of putative toxin gene homologs from Russell’s viper (Daboia russelii) using whole-genome sequencing data obtained from shed skin. When compared with the major venom proteins in Russell’s viper studied previously, we found 45–100% sequence similarity between the venom proteins and their putative homologs in the skin. Additionally, comparative analyses of 20 putative toxin gene family homologs provided evidence of unique sequence motifs in nerve growth factor (NGF), platelet derived growth factor (PDGF), Kunitz/Bovine pancreatic trypsin inhibitor (Kunitz BPTI), cysteine-rich secretory proteins, antigen 5, andpathogenesis-related1 proteins (CAP) and cysteine-rich secretory protein (CRISP). In those derived proteins, we identified V11 and T35 in the NGF domain; F23 and A29 in the PDGF domain; N69, K2 and A5 in the CAP domain; and Q17 in the CRISP domain to be responsible for differences in the largest pockets across the protein domain structures in crotalines, viperines and elapids from the in silico structure-based analysis. Similarly, residues F10, Y11 and E20 appear to play an important role in the protein structures across the kunitz protein domain of viperids and elapids. Our study highlights the usefulness of shed skin in obtaining good quality high-molecular weight DNA for comparative genomic studies, and provides evidence towards the unique features and evolution of putative venom gene homologs in vipers.

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Proteomic and functional analyses of the venom of Porthidium lansbergii lansbergii (Lansberg's hognose viper) from the Atlantic Department of Colombia

Cited by 37 publications

References 36 publications

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

Gene expression profiling of the venom gland from the Venezuelan mapanare (Bothrops colombiensis) using expressed sequence tags (ESTs)

Comparative analyses of putative toxin gene homologs from an Old World viper,Daboia russelii

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