Identification of Venom Proteins of the Indigenous Endoparasitoid Chouioia cunea (Hymenoptera: Eulophidae)

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.

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Snake Venom Proteins: Development into Antimicrobial and Wound Healing Agents

Mini-Reviews in Organic Chemistry ◽

10.2174/1570193x1101140402100131 ◽

2014 ◽

Vol 11 (1) ◽

pp. 4-14 ◽

Cited By ~ 8

Author(s):

Ramar Samy ◽

Jayapal Manikandan ◽

Gautam Sethi ◽

Octavio Franco ◽

Josiah C. Okonkwo ◽

...

Keyword(s):

Wound Healing ◽

Snake Venom ◽

Venom Proteins

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Identification of a Novel Family of Snake Venom Proteins Veficolins fromCerberus rynchopsUsing a Venom Gland Transcriptomics and Proteomics Approach

Journal of Proteome Research ◽

10.1021/pr901044x ◽

2010 ◽

Vol 9 (4) ◽

pp. 1882-1893 ◽

Cited By ~ 60

Author(s):

G. OmPraba ◽

Alex Chapeaurouge ◽

Robin Doley ◽

K. Rama Devi ◽

P. Padmanaban ◽

...

Keyword(s):

Snake Venom ◽

Venom Gland ◽

Proteomics Approach ◽

Venom Proteins

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Inferring Species Trees from Gene Trees: A Phylogenetic Analysis of the Elapidae (Serpentes) Based on the Amino Acid Sequences of Venom Proteins

Molecular Phylogenetics and Evolution ◽

10.1006/mpev.1997.0434 ◽

1997 ◽

Vol 8 (3) ◽

pp. 349-362 ◽

Cited By ~ 79

Author(s):

Joseph B Slowinski ◽

Alec Knight ◽

Alejandro P Rooney

Keyword(s):

Phylogenetic Analysis ◽

Amino Acid ◽

Amino Acid Sequences ◽

Gene Trees ◽

Species Trees ◽

Venom Proteins

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Venomics of the Australian eastern brown snake ( Pseudonaja textilis ): Detection of new venom proteins and splicing variants

Toxicon ◽

10.1016/j.toxicon.2015.06.005 ◽

2015 ◽

Vol 107 ◽

pp. 252-265 ◽

Cited By ~ 18

Author(s):

Vincent Louis Viala ◽

Diana Hildebrand ◽

Maria Trusch ◽

Tamara Mieco Fucase ◽

Juliana Mozer Sciani ◽

...

Keyword(s):

Splicing Variants ◽

Venom Proteins

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Parasitoid wasp venom targets host immune cell production in a Drosophila-parasitoid interaction

10.1101/2020.12.01.406736 ◽

2020 ◽

Author(s):

Jordann E. Trainor ◽

KR Pooja ◽

Nathan T. Mortimer

Keyword(s):

Immune Cell ◽

Sequence Data ◽

Parasitoid Wasp ◽

National Institutes Of Health ◽

Medical Sciences ◽

Host Signaling ◽

Jnk Signaling Pathway ◽

Host Parasite ◽

Host Immune Cell ◽

Venom Proteins

AbstractThe interactions between Drosophila melanogaster and the parasitoid wasps that infect Drosophila species provide an important model for understanding host-parasite relationships. Following parasitoid infection, D. melanogaster larvae mount a response in which immune cells (hemocytes) form a capsule around the wasp egg, which then melanizes leading to death of the parasitoid. Previous studies have found that host hemocyte load, the number of hemocytes available for the encapsulation response, and the production of lamellocytes, an infection induced hemocyte type, are major determinants of host resistance. Parasitoids have evolved various virulence mechanisms to overcome the immune response of the D. melanogaster host, including both active immune suppression by venom proteins and passive immune evasive mechanisms. We find that a previously undescribed parasitoid species, Asobara sp. AsDen, utilizes an active virulence mechanism to infect D. melanogaster hosts. Asobara sp. AsDen infection inhibits host hemocyte expression of msn, a member of the JNK signaling pathway, which plays a role in lamellocyte production. Asobara sp. AsDen infection restricts the production of lamellocytes as assayed by hemocyte cell morphology and altered msn expression. Our findings suggest that Asobara sp. AsDen venom targets host signaling to suppress immunity.DeclarationsFundingThis work was supported by the National Institute of General Medical Sciences of the National Institutes of Health under Award Number R35GM133760.Availability of data and materialSequence data has been deposited in GenBank under accession # MT498809. Custom BLAST databases are available on request to corresponding author.Authors’ contributionsConceived of or designed study: J.E.T., N.T.M.; Performed research: J.E.T., P.K.; Analyzed data: J.E.T., P.K., N.T.M.; Wrote the paper: J.E.T., P.K., N.T.M.

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Cardiovascular Effects of Snake Toxins: Cardiotoxicity and Cardioprotection

Acta Naturae ◽

10.32607/actanaturae.11375 ◽

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.

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TOXIFY: a deep learning approach to classify animal venom proteins

10.7287/peerj.preprints.27498 ◽

2019 ◽

Author(s):

T Jeffrey Cole ◽

Michael S Brewer

Keyword(s):

Protein Sequence ◽

Software Package ◽

Shotgun Proteomics ◽

Learning Approach ◽

The Novel ◽

Venom Protein ◽

Order Of Magnitude ◽

Gated Recurrent Units ◽

Venom Proteins ◽

Generation Sequencing

In the era of Next-Generation Sequencing and shotgun proteomics, the sequences of animal toxigenic proteins are being generated at rates exceeding the pace of traditional means for empirical toxicity verification. To facilitate the automation of toxin identification from protein sequences, we trained Recurrent Neural Networks with Gated Recurrent Units on publicly available datasets. The resulting models are available via the novel software package TOXIFY, allowing users to infer the probability of a given protein sequence being a venom protein. TOXIFY is more than 20X faster and uses over an order of magnitude less memory than previously published methods. Additionally, TOXIFY is more accurate, precise, and sensitive at classifying venom proteins. Availability: https://www.github.com/tijeco/toxify

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Model-based inference of punctuated molecular evolution

10.1101/852343 ◽

2019 ◽

Cited By ~ 1

Author(s):

Marc Manceau ◽

Julie Marin ◽

Hélène Morlon ◽

Amaury Lambert

Keyword(s):

Molecular Evolution ◽

Dna Sequences ◽

Temporal Variations ◽

Multiple Sequence ◽

Model Combining ◽

Constant Rate ◽

Whole Genomes ◽

Standard Models ◽

Natural Variance ◽

Venom Proteins

AbstractIn standard models of molecular evolution, DNA sequences evolve through asynchronous substitutions according to Poisson processes with a constant rate (called the molecular clock) or a time-varying rate (relaxed clock). However, DNA sequences can also undergo episodes of fast divergence that will appear as synchronous substitutions affecting several sites simultaneously at the macroevolutionary time scale. Here, we develop a model combining basal, clock-like molecular evolution with episodes of fast divergence called spikes arising at speciation events. Given a multiple sequence alignment and its time-calibrated species phylogeny, our model is able to detect speciation events (including hidden ones) co-occurring with spike events and to estimate the probability and amplitude of these spikes on the phylogeny. We identify the conditions under which spikes can be distinguished from the natural variance of the clock-like component of molecular evolution and from temporal variations of the clock. We apply the method to genes underlying snake venom proteins and identify several spikes at gene-specific locations in the phylogeny. This work should pave the way for analyses relying on whole genomes to inform on modes of species diversification.

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