Snake Venom Proteins: Development into Antimicrobial and Wound Healing Agents

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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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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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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High throughput screening and identification of coagulopathic snake venom proteins and peptides using nanofractionation and proteomics approaches

PLoS Neglected Tropical Diseases ◽

10.1371/journal.pntd.0007802 ◽

2020 ◽

Vol 14 (4) ◽

pp. e0007802 ◽

Cited By ~ 9

Author(s):

Julien Slagboom ◽

Marija Mladić ◽

Chunfang Xie ◽

Taline D. Kazandjian ◽

Freek Vonk ◽

...

Keyword(s):

Snake Venom ◽

High Throughput ◽

High Throughput Screening ◽

Screening And Identification ◽

Venom Proteins ◽

Proteins And Peptides

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Cysteine-Rich Secretory Proteins (CRISPs) from Venomous Snakes: An Overview of the Functional Diversity in a Large and Underappreciated Superfamily

Toxins ◽

10.3390/toxins12030175 ◽

2020 ◽

Vol 12 (3) ◽

pp. 175 ◽

Cited By ~ 3

Author(s):

Takashi Tadokoro ◽

Cassandra M. Modahl ◽

Katsumi Maenaka ◽

Narumi Aoki-Shioi

Keyword(s):

Snake Venom ◽

Inflammatory Responses ◽

Neutrophil Infiltration ◽

Secretory Proteins ◽

Sequence Alignments ◽

Functional Sites ◽

Accelerated Evolution ◽

Evolutionarily Conserved ◽

Pathogenesis Related ◽

Venom Proteins

The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found in the majority of venoms, very few of these proteins have been functionally characterized, but those that have been exhibit diverse activities. Snake venom CRISPs (svCRISPs) inhibit ion channels and the growth of new blood vessels (angiogenesis). They also increase vascular permeability and promote inflammatory responses (leukocyte and neutrophil infiltration). Interestingly, CRISPs in lamprey buccal gland secretions also manifest some of these activities, suggesting an evolutionarily conserved function. As we strive to better understand the functions that CRISPs serve in venoms, it is worth considering the broad range of CRISP physiological activities throughout the animal kingdom. In this review, we summarize those activities, known crystal structures and sequence alignments, and we discuss predicted functional sites. CRISPs may not be lethal or major components of venoms, but given their almost ubiquitous occurrence in venoms and the accelerated evolution of svCRISP genes, these venom proteins are likely to have functions worth investigating.

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

Toxins ◽

10.3390/toxins11020095 ◽

2019 ◽

Vol 11 (2) ◽

pp. 95 ◽

Cited By ~ 12

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.

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Interaction of uranyl ions with snake venom proteins fromLachesis muta muta

Journal of Radioanalytical and Nuclear Chemistry ◽

10.1007/bf02223382 ◽

1997 ◽

Vol 223 (1-2) ◽

pp. 187-191 ◽

Cited By ~ 1

Author(s):

H. J. MacCordick ◽

F. Taghva ◽

J. -P. Meyer ◽

D. Gelus

Keyword(s):

Snake Venom ◽

Uranyl Ions ◽

Venom Proteins

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

Biochemical Journal ◽

10.1042/bj20130599 ◽

2013 ◽

Vol 455 (2) ◽

pp. 239-250 ◽

Cited By ~ 3

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.

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