The Role of Conventional Two-Dimensional Electrophoresis (2DE) and Its Newer Applications in the Study of Snake Venoms

Vejayan, Jaya; Tang, Mei; Ibrahim, Halijah

doi:10.5772/28717

Cited by 4 publications

(3 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Biological explanation for observed discrepancies would be snake gender, Latinović et al does not declare it, and the snake habitat, in our case venom was obtained from the snakes captured in natural environment in Slovak Republic, or age of snakes and type of food. Influence of these factors was described before and could attribute to the observed differences [11].…”

Section: Discussionmentioning

confidence: 99%

Proteome and Peptidome of Vipera berus berus Venom

et al. 2016

View full text Add to dashboard Cite

Snake venom is a rich source of peptides and proteins with a wide range of actions. Many of the venom components are currently being tested for their usefulness in the treatment of many diseases ranging from neurological and cardiovascular to cancer. It is also important to constantly search for new proteins and peptides with properties not yet described. The venom of Vipera berus berus has hemolytic, proteolytic and cytotoxic properties, but its exact composition and the factors responsible for these properties are not known. Therefore, an attempt was made to identify proteins and peptides derived from this species venom by using high resolution two-dimensional electrophoresis and MALDI ToF/ToF mass spectrometry. A total of 11 protein classes have been identified mainly proteases but also L-amino acid oxidases, C-type lectin like proteins, cysteine-rich venom proteins and phospholipases A 2 and 4 peptides of molecular weight less than 1500 Da. Most of the identified proteins are responsible for the highly hemotoxic properties of the venom. Presence of venom phospholipases A 2 and L-amino acid oxidases cause moderate neuro-, myo-and cytotoxicity. All successfully identified peptides belong to the bradykinin-potentiating peptides family. The mass spectrometry data are available via ProteomeXchange with identifier PXD004958.

show abstract

Section: Discussionmentioning

confidence: 99%

Proteome and Peptidome of Vipera berus berus Venom

et al. 2016

View full text Add to dashboard Cite

show abstract

“…The therapeutic efficacy of the latter depends highly on the amounts of the antibodies that could neutralize the heterologous causative venom components (paraspecificity) [ 6 , 7 ]. Therefore, insight into the venom proteomes of individual venomous snake species that inhabit common geographical areas/localities, like O. hannah and N. kaouthia , which produce similar clinical features [ 7 , 8 ] and the identification of common components shared among their venoms should be useful information for treatment indication when homologous and polyspecific antivenins are not available. In this study, the O. hannah venom proteome was characterized, and the components cross-reactive to horse derived-monospecific N. kaouthia antivenin were determined.…”

Section: Introductionmentioning

confidence: 99%

Ophiophagus hannah Venom: Proteome, Components Bound by Naja kaouthia Antivenin and Neutralization by N. kaouthia Neurotoxin-Specific Human ScFv

Danpaiboon

Reamtong

Sookrung

et al. 2014

Toxins

View full text Add to dashboard Cite

Venomous snakebites are an important health problem in tropical and subtropical countries. King cobra (Ophiophagus hannah) is the largest venomous snake found in South and Southeast Asia. In this study, the O. hannah venom proteome and the venom components cross-reactive to N. kaouthia monospecific antivenin were studied. O. hannah venom consisted of 14 different protein families, including three finger toxins, phospholipases, cysteine-rich secretory proteins, cobra venom factor, muscarinic toxin, L-amino acid oxidase, hypothetical proteins, low cysteine protein, phosphodiesterase, proteases, vespryn toxin, Kunitz, growth factor activators and others (coagulation factor, endonuclease, 5’-nucleotidase). N. kaouthia antivenin recognized several functionally different O. hannah venom proteins and mediated paratherapeutic efficacy by rescuing the O. hannah envenomed mice from lethality. An engineered human ScFv specific to N. kaouthia long neurotoxin (NkLN-HuScFv) cross-neutralized the O. hannah venom and extricated the O. hannah envenomed mice from death in a dose escalation manner. Homology modeling and molecular docking revealed that NkLN-HuScFv interacted with residues in loops 2 and 3 of the neurotoxins of both snake species, which are important for neuronal acetylcholine receptor binding. The data of this study are useful for snakebite treatment when and where the polyspecific antivenin is not available. Because the supply of horse-derived antivenin is limited and the preparation may cause some adverse effects in recipients, a cocktail of recombinant human ScFvs for various toxic venom components shared by different venomous snakes, exemplified by the in vitro produced NkLN-HuScFv in this study, should contribute to a possible future route for an improved alternative to the antivenins.

show abstract

“…Earlier the presence of these two groups in almost equal amounts was reported [4], whereas in our case there is twice as much phospholipases than metalloproteinases. These differences may be due to many factors: gender, age of snakes, geographical origin or type of food [19]. As shown in our previous work, the differences may also occur when other analytical techniques are used to analyze the venom composition (RP-HPLC + SDS-PAGE vs. 2DE) [20].…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analyses of Agkistrodon contortrix contortrix Venom Using 2D Electrophoresis and MS Techniques

Bocian

Urbanik

Hus

et al. 2016

Toxins

View full text Add to dashboard Cite

Snake venom is a complex mixture of proteins and peptides which in the Viperidae is mainly hemotoxic. The diversity of these components causes the venom to be an extremely interesting object of study. Discovered components can be used in search for new pharmaceuticals used primarily in the treatment of diseases of the cardiovascular system. In order to determine the protein composition of the southern copperhead venom, we have used high resolution two dimensional electrophoresis and MALDI ToF/ToF MS-based identification. We have identified 10 groups of proteins present in the venom, of which phospholipase A2 and metalloprotease and serine proteases constitute the largest groups. For the first time presence of 5′-nucleotidase in venom was found in this group of snakes. Three peptides present in the venom were also identified. Two of them as bradykinin-potentiating agents and one as an inhibitor.

show abstract

The Role of Conventional Two-Dimensional Electrophoresis (2DE) and Its Newer Applications in the Study of Snake Venoms

Cited by 4 publications

References 56 publications

Proteome and Peptidome of Vipera berus berus Venom

Proteome and Peptidome of Vipera berus berus Venom

Ophiophagus hannah Venom: Proteome, Components Bound by Naja kaouthia Antivenin and Neutralization by N. kaouthia Neurotoxin-Specific Human ScFv

Proteomic Analyses of Agkistrodon contortrix contortrix Venom Using 2D Electrophoresis and MS Techniques

Contact Info

Product

Resources

About