Proteopeptidomic, Functional and Immunoreactivity Characterization of Bothrops moojeni Snake Venom: Influence of Snake Gender on Venom Composition

Amorim, Fernanda Gobbi; Costa, Tássia R.; Baiwir, Dominique; Pauw, Edwin De; Quinton, Loïc; Sampaio, Suely Vilela

doi:10.3390/toxins10050177

Cited by 54 publications

(41 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This was also reflected in the pools: male pool had a higher activity than female pool. Similar results were also observed in other species, like B. jararaca and B. moojeni [34,77]. This result was corroborated by mass spectrometry identification, in which a higher percentage of PLA 2 was found in the male pool.…”

Section: Functional Analysissupporting

confidence: 87%

“…However, male venom pool showed higher activity compared to the female pool ( Figure 3C). Although contrasting, the same behavior was observed in B. moojeni [34]. Similar to collagenolytic activity, LAAO activity differed individually.…”

Section: Functional Analysissupporting

confidence: 57%

“…Individual variability is a well-established concept when referring to intraspecific variation of snake venom composition and/or its activities, and may be related to ontogeny [23][24][25], diet [26,27], seasonality [28], geographical location [29][30][31], gender [32][33][34][35], and captivity [22,36]. Within the Bothrops species, B. jararaca venom is the most studied one regarding gender differences [32,37], contrary from B. atrox, despite its high geographic distribution and epidemiological representation.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Venom complexity of Bothrops atrox (common lancehead) siblings

Hatakeyama

Tasima

Bravo-Tobar

et al. 2020

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

Background: Variability in snake venoms is a well-studied phenomenon. However, sex-based variation of Bothrops atrox snake venom using siblings is poorly investigated. Bothrops atrox is responsible for the majority of snakebite accidents in the Brazilian Amazon region. Differences in the venom composition of Bothrops genus have been linked to several factors such as ontogeny, geographical distribution, prey preferences and sex. Thus, in the current study, venom samples of Bothrops atrox male and female siblings were analyzed in order to compare their biochemical and biological characteristics. Methods: Venoms were collected from five females and four males born from a snake captured from the wild in São Bento (Maranhão, Brazil), and kept in the Laboratory of Herpetology of Butantan Intitute. The venoms were analyzed individually and as a pool of each gender. The assays consisted in protein quantification, 1-DE, mass spectrometry, proteolytic, phospholipase A 2 , L-amino acid oxidase activities, minimum coagulant dose upon plasma, minimum hemorrhagic dose and lethal dose 50%. Results: Electrophoretic profiles of male's and female's venom pools were quite similar, with minor sex-based variation. Male venom showed higher LAAO, PLA 2 and hemorrhagic activities, while female venom showed higher coagulant activity. On the other hand, the proteolytic activities did not show statistical differences between pools, although some individual variations were observed. Meanwhile, proteomic profile revealed 112 different protein compounds; of which 105 were common proteins of female's and male's venom pools and seven were unique to females. Despite individual variations, lethality of both pools showed similar values. Conclusion: Although differences between female and male venoms were observed, our results show that individual variations are significant even between siblings, highlighting that biological activities of venoms and its composition are influenced by other factors beyond gender.

show abstract

Section: Functional Analysissupporting

confidence: 87%

Section: Functional Analysissupporting

confidence: 57%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Venom complexity of Bothrops atrox (common lancehead) siblings

Hatakeyama

Tasima

Bravo-Tobar

et al. 2020

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

show abstract

“…These enzymes are not toxic themselves, but potentiate the effect of ion channel toxins present in venoms, acting as spreading factors [ 69 ]. Hyaluronidases have been identified in many animal venoms, such as those of insects [ 70 ], arachnids [ 8 , 18 , 19 , 71 , 72 ], and snakes [ 73 ]. We found three transcripts that putatively code for hyaluronidases, of which only transcript SgeEnzHya01 was recovered with the complete CDS ( Supplementary Table S1 ).…”

Section: Resultsmentioning

confidence: 99%

Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi

Romero-Gutiérrez

Santibáñez‐López

Jiménez-Vargas

et al. 2018

Toxins

View full text Add to dashboard Cite

To understand the diversity of scorpion venom, RNA from venomous glands from a sawfinger scorpion, Serradigitus gertschi, of the family Vaejovidae, was extracted and used for transcriptomic analysis. A total of 84,835 transcripts were assembled after Illumina sequencing. From those, 119 transcripts were annotated and found to putatively code for peptides or proteins that share sequence similarities with the previously reported venom components of other species. In accordance with sequence similarity, the transcripts were classified as potentially coding for 37 ion channel toxins; 17 host defense peptides; 28 enzymes, including phospholipases, hyaluronidases, metalloproteases, and serine proteases; nine protease inhibitor-like peptides; 10 peptides of the cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 protein superfamily; seven La1-like peptides; and 11 sequences classified as “other venom components”. A mass fingerprint performed by mass spectrometry identified 204 components with molecular masses varying from 444.26 Da to 12,432.80 Da, plus several higher molecular weight proteins whose precise masses were not determined. The LC-MS/MS analysis of a tryptic digestion of the soluble venom resulted in the de novo determination of 16,840 peptide sequences, 24 of which matched sequences predicted from the translated transcriptome. The database presented here increases our general knowledge of the biodiversity of venom components from neglected non-buthid scorpions.

show abstract

“…As several studies have shown correlations between different ecological, geographical, genetic and/or developmental factors and the venom proteome, e.g. different diets [30][31][32][33], regional separation of populations [10,[34][35][36], sex [37][38][39] or age [40][41][42][43] it would be ideal to characterize venom composition from a representative cohort of individual animals. However, due to the time consuming nature and expensive costs associated with de-complexing bottom-up venom analysis, most venom compositions reported so far [16], were analyzed from a single pool of venom that was sourced from different numbers of individuals.…”

Section: Introductionmentioning

confidence: 99%