“…This is much higher than the amount of PLA2s present in Pakistani N. naja . A proteomic study of N. kaouthia venom reported PLA 2 s as one of the most abundant venom proteins [ 74 ]. While another study on the venom proteome of N. annulifera did not detect PLA 2 s [ 75 ].…”
Section: Discussionmentioning
confidence: 99%
“…The present study shows that N. naja and N. oxiana snake venom contain significant amounts of metalloproteinases, which are the second most abundant protein family. Proteomics study of other Naja species shows the presence of SVMPs in varying amounts ranging from as low as 0.9% to 16% [ 74 , 92 , 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 ]. Previous proteomic studies reported a lower abundance of SVMP in Pakistani N. naja venom [ 42 , 43 , 44 ].…”
Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus Naja i.e., Naja naja (black cobra) and Naja oxiana (brown cobra) of Pakistani origin. The present study has shown that these snake venoms consist of a highly diversified proteome. Furthermore, the data also revealed variation among closely related species. High throughput mass spectrometric analysis of the venom proteome allowed to identify for the N. naja venom 34 protein families and for the N. oxiana 24 protein families. The comparative evaluation of the two venoms showed that N. naja consists of a more complex venom proteome than N. oxiana venom. Analysis also showed N-terminal acetylation (N-ace) of a few proteins in both venoms. To the best of our knowledge, this is the first study revealing this posttranslational modification in snake venom. N-ace can shed light on the mechanism of regulation of venom proteins inside the venom gland. Furthermore, our data showed the presence of other body proteins, e.g., ankyrin repeats, leucine repeats, zinc finger, cobra serum albumin, transferrin, insulin, deoxyribonuclease-2-alpha, and other regulatory proteins in these venoms. Interestingly, our data identified Ras-GTpase type of proteins, which indicate the presence of extracellular vesicles in the venom. The data can support the production of distinct and specific anti-venoms and also allow a better understanding of the envenomation and mechanism of distribution of toxins. Data are available via ProteomeXchange with identifier PXD018726.
“…This is much higher than the amount of PLA2s present in Pakistani N. naja . A proteomic study of N. kaouthia venom reported PLA 2 s as one of the most abundant venom proteins [ 74 ]. While another study on the venom proteome of N. annulifera did not detect PLA 2 s [ 75 ].…”
Section: Discussionmentioning
confidence: 99%
“…The present study shows that N. naja and N. oxiana snake venom contain significant amounts of metalloproteinases, which are the second most abundant protein family. Proteomics study of other Naja species shows the presence of SVMPs in varying amounts ranging from as low as 0.9% to 16% [ 74 , 92 , 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 ]. Previous proteomic studies reported a lower abundance of SVMP in Pakistani N. naja venom [ 42 , 43 , 44 ].…”
Latest advancement of omics technologies allows in-depth characterization of venom compositions. In the present work we present a proteomic study of two snake venoms of the genus Naja i.e., Naja naja (black cobra) and Naja oxiana (brown cobra) of Pakistani origin. The present study has shown that these snake venoms consist of a highly diversified proteome. Furthermore, the data also revealed variation among closely related species. High throughput mass spectrometric analysis of the venom proteome allowed to identify for the N. naja venom 34 protein families and for the N. oxiana 24 protein families. The comparative evaluation of the two venoms showed that N. naja consists of a more complex venom proteome than N. oxiana venom. Analysis also showed N-terminal acetylation (N-ace) of a few proteins in both venoms. To the best of our knowledge, this is the first study revealing this posttranslational modification in snake venom. N-ace can shed light on the mechanism of regulation of venom proteins inside the venom gland. Furthermore, our data showed the presence of other body proteins, e.g., ankyrin repeats, leucine repeats, zinc finger, cobra serum albumin, transferrin, insulin, deoxyribonuclease-2-alpha, and other regulatory proteins in these venoms. Interestingly, our data identified Ras-GTpase type of proteins, which indicate the presence of extracellular vesicles in the venom. The data can support the production of distinct and specific anti-venoms and also allow a better understanding of the envenomation and mechanism of distribution of toxins. Data are available via ProteomeXchange with identifier PXD018726.
“…The antivenomic analysis approach based on venomic pro le, originally developed as an in vitro platform to qualitatively and quantitatively assess the e cacy of antivenom, has since been updated to the 3rd generation and displays a powerful potential as a substitute for many traditional strategies to evaluate antivenom e cacy [32]. Similar to several recently reported studies using 3rd generation antivenomics [53][54][55], the immunocapture capacity of antivenoms in the present study increased as the incubation amount of H. curtus venom increased but varied according to different venom components. Overall, N. atra antivenom exhibited higher capacity to immunocapture whole H. curtus venom than B. multicinctus antivenom, especially for SNX, PLA 2 , and CRISP.…”
Background: A comprehensive evaluation of the -omic profiles of venom is important for understanding the potential function and evolution of snake venom. Here, we conducted an integrated multi-omics-analysis to unveil the venom-transcriptomic and venomic profiles in a same group of spine-bellied sea snakes (Hydrophis curtus) from the South China Sea, where the snake is a widespread species and might generate regionally-specific venom potentially harmful to human activities. The capacity of two heterologous antivenoms to immunocapture the H. curtus venom was determined for an in-depth evaluation of their rationality in treatment of H. curtus envenomation. In addition, a phylogenetic analysis by maximum likelihood was used to detect the adaptive molecular evolution of full-length toxin-coding unigenes.Results: A total of 90,909,384 pairs of clean reads were generated via Illumina sequencing from a pooled cDNA library of six specimens, and yielding 148,121 unigenes through de novo assembly. Sequence similarity searching harvested 63,845 valid annotations, including 63,789 non-toxin-coding and 56 toxin-coding unigenes belonging to 22 protein families. Three protein families, three-finger toxins (3-FTx), phospholipase A2 (PLA2), and cysteine-rich secretory protein, were detected in the venom proteome. 3-FTx (27.15% in the transcriptome/41.94% in the proteome) and PLA2 (59.71%/49.36%) were identified as the most abundant families in the venom-gland transcriptome and venom proteome. In addition, 24 unigenes from 11 protein families were shown to have experienced positive selection in their evolutionary history, whereas four were relatively conserved throughout evolution. Commercial Naja atra antivenom exhibited a stronger capacity than Bungarus multicinctus antivenom to immunocapture H. curtus venom components, especially short neurotoxins, with the capacity of both antivenoms to immunocapture short neurotoxins being weaker than that for PLA2s.Conclusions: Our study clarified the venom-gland transcriptomic and venomic profiles along with the within-group divergence of a H. curtus population from the South China Sea. Adaptive evolution of most venom components driven by natural selection appeared to occur rapidly during evolutionary history. Notably, the utility of commercial N. atra and B. multicinctus antivenoms against H. curtus toxins was not comprehensive; thus, the development of species-specific antivenom is urgently needed.
“…Venom metabolomics is a developing field of research, which provides an opportunity to explore new low-molecular-weight compounds by using modern approaches, such as mass spectrometry-based methodologies [19]. Venomics studies are still focused on the protein and peptide components of venoms and secretions [22][23][24]. Using the tag 'venom proteomics' on the PubMed engine obtained 730 results while using 'venom metabolomics' obtained only 23 results.…”
Organic acids are important active small molecules present in venoms and toxins, which have not been fully explored yet. The aim of the study was the determination of organic acids in honeybee venom (HBV) samples by using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Two protocols for sample preparation were employed. A solid-phase extraction was used for the determination of malonic acid, fumaric acid, glutaric acid, and kynurenic acid. A dilute-and-shoot method was optimal for: citric acid, malic acid, and succinic acid. Chromatographic separation was performed using a Synergi Hydro-RP column. Detection was performed on a triple-quadrupole mass spectrometer operating in multiple reaction monitoring mode. Among the analytes, glutaric acid and kynurenic acid were present in HBV samples in the lowest concentrations, whereas citric acid was the most abundant acid in each sample, and accounted for an average of 86 mg/g (8.6%) of the venom dry weight. Organic acids were discussed in terms of function. This is the first study in the available literature that provides specific data on the content of organic acids in HBV using a validated quantitative method.Key Contribution: The first study that provided specific and accurate data on the content of a panel of low-molecular-weight organic acids in honeybee venom.
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