Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong
Keyword(s):  
Snake Venom ◽  
Protein Families ◽  
Traditional Medicines ◽  
Phospholipases A2 ◽  
Inhibitory Peptides ◽  
Sds Page ◽  
Deinagkistrodon Acutus ◽  
Venom Proteins ◽  
Proteins And Peptides

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.

scholarly journals Cardiovascular Effects of Snake Toxins: Cardiotoxicity and Cardioprotection

Acta Naturae ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 4-14
Author(s):  
Alexey S. Averin ◽  
Yuri N. Utkin
Keyword(s):  
Cardiovascular System ◽  
Snake Venom ◽  
Antihypertensive Drugs ◽  
Cardiovascular Effects ◽  
Medical Application ◽  
New Drugs ◽  
Snake Venoms ◽  
Phospholipases A2 ◽  
Venom Proteins ◽  
Proteins And Peptides

Snake venoms, as complex mixtures of peptides and proteins, affect various vital systems of the organism. One of the main targets of the toxic components from snake venoms is the cardiovascular system. Venom proteins and peptides can act in different ways, exhibiting either cardiotoxic or cardioprotective effects. The principal classes of these compounds are cobra cardiotoxins, phospholipases A2, and natriuretic, as well as bradykinin-potentiating peptides. There is another group of proteins capable of enhancing angiogenesis, which include, e.g., vascular endothelial growth factors possessing hypotensive and cardioprotective activities. Venom proteins and peptides exhibiting cardiotropic and vasoactive effects are promising candidates for the design of new drugs capable of preventing or constricting the development of pathological processes in cardiovascular diseases, which are currently the leading cause of death worldwide. For example, a bradykinin-potentiating peptide from Bothrops jararaca snake venom was the first snake venom compound used to create the widely used antihypertensive drugs captopril and enalapril. In this paper, we review the current state of research on snake venom components affecting the cardiovascular system and analyse the mechanisms of physiological action of these toxins and the prospects for their medical application.

scholarly journals Venomics of Trimeresurus (Popeia) nebularis, the Cameron Highlands Pit Viper from Malaysia: Insights into Venom Proteome, Toxicity and Neutralization of Antivenom

Toxins ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 95 ◽  
Author(s):  
Choo Tan ◽  
Kae Tan ◽  
Tzu Ng ◽  
Evan Quah ◽  
Ahmad Ismail ◽  
...  
Keyword(s):  
Snake Venom ◽  
Serine Proteases ◽  
Cross Reactivity ◽  
Secretory Proteins ◽  
Proteomic Profiling ◽  
Phospholipases A2 ◽  
Central Highland ◽  
Liquid Chromatography Tandem Mass ◽  
Cameron Highlands ◽  
Venom Proteins

Trimeresurus nebularis is a montane pit viper that causes bites and envenomation to various communities in the central highland region of Malaysia, in particular Cameron’s Highlands. To unravel the venom composition of this species, the venom proteins were digested by trypsin and subjected to nano-liquid chromatography-tandem mass spectrometry (LC-MS/MS) for proteomic profiling. Snake venom metalloproteinases (SVMP) dominated the venom proteome by 48.42% of total venom proteins, with a characteristic distribution of P-III: P-II classes in a ratio of 2:1, while P-I class was undetected. Snaclecs constituted the second most venomous protein family (19.43%), followed by snake venom serine proteases (SVSP, 14.27%), phospholipases A2 (5.40%), disintegrins (5.26%) and minor proteins including cysteine-rich secretory proteins, L-amino acid oxidases, phosphodiesterases, 5′-nucleotidases. The venomic profile correlates with local (painful progressive edema) and systemic (hemorrhage, coagulopathy, thrombocytopenia) manifestation of T. nebularis envenoming. As specific antivenom is unavailable for T. nebularis, the hetero-specific Thai Green Pit viper Monovalent Antivenom (GPVAV) was examined for immunological cross-reactivity. GPVAV exhibited good immunoreactivity to T. nebularis venom and the antivenom effectively cross-neutralized the hemotoxic and lethal effects of T. nebularis (lethality neutralizing potency = 1.6 mg venom per mL antivenom). The findings supported GPVAV use in treating T. nebularis envenoming.

Characterization of inflamin, the first member of a new family of snake venom proteins that induces inflammation

2013 ◽  
Vol 455 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Bhaskar Barnwal ◽  
R. Manjunatha Kini
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Calcium Dependent ◽  
Venom Toxin ◽  
New Family ◽  
Snake Venom Toxin ◽  
Venom Proteins

Inflamin, a novel snake venom toxin from Aipysurus eydouxii, leads to the activation of calcium-dependent phospholipase A2 by phosphorylation at Ser505, resulting in inflammation and pain.

scholarly journals Molecular Characterization of Lys49 and Asp49 Phospholipases A2 from Snake Venom and Their Antiviral Activities against Dengue virus

Toxins ◽  
2013 ◽  
Vol 5 (10) ◽  
pp. 1780-1798 ◽  
Author(s):  
Alzira Cecilio ◽  
Sergio Caldas ◽  
Raiana Oliveira ◽  
Arthur Santos ◽  
Michael Richardson ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Molecular Characterization ◽  
Snake Venom ◽  
Phospholipases A2 ◽  
Antiviral Activities

scholarly journals Proteo-Transcriptomic Characterization of the Venom from the Endoparasitoid Wasp Pimpla turionellae with Aspects on Its Biology and Evolution

Toxins ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 721 ◽  
Author(s):  
Rabia Özbek ◽  
Natalie Wielsch ◽  
Heiko Vogel ◽  
Günter Lochnit ◽  
Frank Foerster ◽  
...  
Keyword(s):  
Transcriptome Assembly ◽  
Parasitoid Wasp ◽  
Venom Gland ◽  
Hymenopteran Species ◽  
Robber Flies ◽  
And Function ◽  
Wasp Venoms ◽  
Venom Proteins ◽  
Proteins And Peptides

Within mega-diverse Hymenoptera, non-aculeate parasitic wasps represent 75% of all hymenopteran species. Their ovipositor dual-functionally injects venom and employs eggs into (endoparasitoids) or onto (ectoparasitoids) diverse host species. Few endoparasitoid wasps such as Pimpla turionellae paralyze the host and suppress its immune responses, such as encapsulation and melanization, to guarantee their offspring’s survival. Here, the venom and its possible biology and function of P. turionellae are characterized in comparison to the few existing proteo-transcriptomic analyses on parasitoid wasp venoms. Multiple transcriptome assembly and custom-tailored search and annotation strategies were applied to identify parasitoid venom proteins. To avoid false-positive hits, only transcripts were finally discussed that survived strict filter settings, including the presence in the proteome and higher expression in the venom gland. P. turionella features a venom that is mostly composed of known, typical parasitoid enzymes, cysteine-rich peptides, and other proteins and peptides. Several venom proteins were identified and named, such as pimplin2, 3, and 4. However, the specification of many novel candidates remains difficult, and annotations ambiguous. Interestingly, we do not find pimplin, a paralytic factor in Pimpla hypochondriaca, but instead a new cysteine inhibitor knot (ICK) family (pimplin2), which is highly similar to known, neurotoxic asilid1 sequences from robber flies.

Preliminary Biochemical and Venomic Characterization of the Venom of Phalotris lemniscatus (Serpentes, Colubridae)

2019 ◽  
Vol 19 (22) ◽  
pp. 1981-1989 ◽  
Author(s):  
Jeny Bastida ◽  
Alejandro Crampet ◽  
Melitta Meneghel ◽  
Victor Morais
Keyword(s):  
Amino Acid ◽  
Blood Coagulation ◽  
Snake Venom ◽  
Clinical Relevance ◽  
Protein Families ◽  
Snake Venoms ◽  
Highly Active ◽  
Venom Composition ◽  
Kunitz Type

Background: For many decades, research on snake venom toxinology focused mainly on the venoms of Viperidae and Elapidae species, which were traditionally the only ones considered as venomous. However, much less interest has been given to the venom produced by opisthoglyphous colubrid snakes, since they were typically considered of no clinical relevance. Objective: The aim of this work is to perform a preliminary biochemical and venomic characterization of the venom of the colubrid snake Phalotris lemniscatus, a species that has been responsible for two relevant cases of envenomation in Uruguay. Methods: We extracted venom from collected specimens and performed different biochemical and proteomic assays to understand its toxin composition. Results: We found that the venom of P. lemniscatus is composed of protein families typically present in snake venoms, such as metallo and serine preoteases, L-amino acid oxidases, phospholipases A2s, Ctype lectines-like, Kunitz-type proteins and three-finger toxins. Activity assays demonstrated a highly active gelatinolytic component as well as a potent capability to induce blood coagulation. Conclusion: The results indicate that the venom of P. lemniscatus contains hemotoxic activities and components that resemble those found in Viperidae (Bothrops) snakes and that can induce a clinically relevant accident. Further studies are needed to better understand the venom composition of this colubrid snake and its most active compounds.

scholarly journals Unmasking Snake Venom ofBothrops leucurus: Purification and Pharmacological and Structural Characterization of New PL Bleu TX-III

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Fábio André Marangoni ◽  
Luis Alberto Ponce-Soto ◽  
Sergio Marangoni ◽  
Elen Cristina Teizem Landucci
Keyword(s):  
Snake Venom ◽  
Intravenous Route ◽  
Systemic Action ◽  
Phospholipid Hydrolysis ◽  
Multiple Alignments ◽  
Sds Page ◽  
One Step ◽  
High Degree

Bleu TX-III was isolated fromBothrops leucurussnake venom on one-step analytical chromatography reverse phase HPLC, was homogeneous on SDS-PAGE, and was confirmed by Q-Tof Ultima API ESI/MS (TOF MS mode) mass spectrometry in 14243.8 Da. Multiple alignments of Bleu TX-III show high degree of homology with basic PLA2myotoxins from otherBothropsvenoms. Our studies on local and systemic myotoxicity “in vivo” reveal that Bleu TX-III is myotoxin with local but not systemic action due to the decrease in the plasmatic CK levels when Bleu TX-III is administrated by intravenous route in mice (dose 1 and 5 μg). And at a dose of 20 μg myotoxin behaves like a local and systemic action. Bleu TX-III induced moderate marked paw edema, evidencing the local increase in vascular permeability. The inflammatory events induced in the mice (I.M.) were investigated. The increase in the levels of IL-1, IL-6, and TNF-αwas observed in the plasma. It is concluded that Bleu TX-III induces inflammatory events in this model. The enzymatic phospholipid hydrolysis may be relevant to these phenomena.Bothrops leucurusvenom is still not extensively explored, and the knowledge of its toxins separately through the study of structure/function will contribute for a better understanding of its action mechanism.

scholarly journals Molecular cloning and characterization of a neurotoxic phospholipase A2 from the venom of Taiwan habu (Trimeresurus mucrosquamatus)

1995 ◽  
Vol 311 (3) ◽  
pp. 895-900 ◽  
Author(s):  
I H Tsai ◽  
P J Lu ◽  
Y M Wang ◽  
C L Ho ◽  
L L Liaw
Keyword(s):  
Gel Filtration ◽  
Rabbit Antiserum ◽  
Cdna Sequencing ◽  
Crude Venom ◽  
Phospholipases A2 ◽  
Sequencing Method ◽  
Sds Page ◽  
Filtration Experiment ◽  
Chick Biventer Cervicis Muscle

Using gel-filtration chromatography and reverse-phase (RP) HPLC we have purified a presynaptic neurotoxin (designated as trimucrotoxin) from the crude venom of Taiwan habu (Trimeresurus mucrosquamatus). Its complete primary structure was solved by an automated N-terminal sequencing and cDNA sequencing method. The enzyme inhibited the twitch of the chick biventer cervicis muscle at 0.1-1 micrograms/ml and showed lethality in mice (LD50 = 1.2 micrograms/g, when given intravenously). Trimucrotoxin exists mainly as a homodimer of 14 kDa subunits as shown by a gel-filtration experiment, and dissociates into monomers during SDS/PAGE in the absence of Ca2+. However, most of trimucrotoxin migrated as slowly as a trimer during nondenaturing SDS/PAGE in the presence of Ca2+ or Sr2+. Its amino acid sequence identity to crotoxin B and agkistrodotoxin is about 75%, and its cDNA sequence is 82% identical to that of crotoxin B. Rabbit antiserum against trimucrotoxin also cross-reacted with the other crotalid neurotoxic phospholipases A2. Furthermore, the purified acidic subunit of crotoxin potentiated the neurotoxicity of trimucrotoxin. A comparison of the sequences of these crotalid neurotoxins revealed some common features of the possible neurotoxic sites, including residues 6, 11, 76-81 and 119-125.

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