Cytotoxic Activities of the Crude Venoms of Macrovipera lebetina lebetina from Cyprus and M. l. obtusa from Turkey (Serpentes: Viperidae) on Human Umbilical Vein Endothelial Cells

İğci, Naşit; Demiralp, F. Duygu Özel; Yıldız, Mehmet Zülfü

doi:10.31594/commagene.655929

Cited by 4 publications

(2 citation statements)

References 22 publications

(28 reference statements)

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“…As a result, major structures were found as random coil and α-helix, taking contributions from β-sheet structures. This finding is concordant with three dimensional structures of snake venom C-type lectins (55), phospholipase A 2 s (56), metalloproteinases (57), and serine proteinases (58), which are also the most abundant proteins in the venom of M. lebetina (3,25,59). Each species has a unique combination of proteins in their venoms and this method can be used to obtain information reflecting the dominant secondary structures of abundant venom proteins, as well as to make comparisons between different species and individuals.…”

Section: Discussionsupporting

confidence: 76%

A Fourier Transform Infrared Spectroscopic Investigation of Macrovipera lebetina lebetina and M. l. obtusa Crude Venoms

İğci¹,

Demiralp²

2020

Eur J Biol

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Objective: Snake venoms are rich sources of bioactive molecules and have been investigated using various bioanalytical methods. Fourier transform infrared (FTIR) spectroscopy is a sensitive method that can be used to analyze biological samples. The aim of this study is to apply the FTIR spectroscopy method for the characterization of snake venom. Materials and Methods:The study characterized the lyophilized crude venoms of Macrovipera lebetina lebetina and M. l. obtusa by FTIR spectroscopy coupled with attenuated total reflectance (ATR) method in the mid-infrared region and compared the spectra between the two subspecies. The band area and intensity values were calculated for comparison and wavenumbers were detected by automated peak picking. Additionally, the study analyzed the secondary structure of venom proteins by using the second derivative spectra. Results:The study detected fourteen major and minor peaks in absorbance spectra which were assigned to various biomolecules such as proteins, carbohydrates, and nucleic acids. Four major sub-bands were observed in the second derivative spectra of Amide I-II region indicating different protein secondary structures. It was observed that there are some quantitative differences and peak shifts between the spectra of venoms of two subspecies, indicating the alteration of biomolecules. Conclusion:To the best of our knowledge, this is the first report of the use of the FTIR-ATR spectroscopy method focusing solely on the characterization of crude snake venoms in literature, accompanied with detailed peak assignment and protein secondary structure analysis. As a preliminary reference study, the results showed the usefulness of FTIR-ATR spectroscopy for the physicochemical characterization of lyophilized snake venom.

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Section: Discussionsupporting

confidence: 76%

A Fourier Transform Infrared Spectroscopic Investigation of Macrovipera lebetina lebetina and M. l. obtusa Crude Venoms

İğci¹,

Demiralp²

2020

Eur J Biol

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“…Viperid venoms are rich in enzymes and nonenzymatic proteins and peptides, many of which interfere with hemostasis [2,3]. Moreover, these venoms have significant cytotoxic activity [1,4,5]. Viperid venom proteins and peptides can be grouped into several major protein families: enzymes such as snake venom serine proteinases (SVSPs), snake venom Zn 2+ -metalloproteinases (SVMPs), L-amino acid oxidases (LAAOs), 5'-nucleotidases, hyaluronidases, group II phospholipase A2s (PLA2s) and proteins without enzymatic activity, namely the disintegrins, C-type lectin proteins (CLPs), cysteinerich secretory proteins (CRISPs), nerve growth factors (NGFs), vascular endothelial growth factors (VEGFs), cystatin, natriuretic peptides and Kunitz-type proteinase inhibitors [1,6].…”

Section: Introductionmentioning

confidence: 99%

Determination of the fibrinogenolytic activity of Montivipera raddei (Raddeʼs mountain viper) venom

Atasoy

İğci

2022

ARCH BIOL SCI BELGRA

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Snake venom fibrinogenolytic enzymes have diagnostic and therapeutic value and are important for snakebite pathology. In the present study, the fibrinogenolytic activity of Montivipera raddei venom was investigated. Crude venom was incubated with human fibrinogen for different times at 37?C. An inhibition study was carried out using different protease inhibitors. The fibrinogenolytic activity was assessed by SDS-PAGE and fibrinogen zymography. An HPLC-based method was used to obtain confirmatory data. Montivipera raddei venom predominantly cleaved the A? chain of fibrinogen in a time-dependent manner. A very slight decrease in band intensity of the B? chain was observable after a longer incubation time. Cleavage of fibrinogen was confirmed by HPLC. Zymography revealed that the venom contained 50 and 75 kDa fibrinogenolytic enzymes. Ethylenediaminetetraacetic acid (EDTA) and 1,10-phenanthroline inhibited the overall fibrinogenolytic activity, while phenylmethylsulfonyl fluoride (PMSF) and aprotinin only inhibited the degradation of the B? chain. These results indicated that metalloproteinases were major fibrinogenolytic enzymes in the venom. An inhibitor study suggested the presence of serine proteinases that broke down the B? chain. With this study, the fibrinogenolytic activity of M. raddei venom was shown for the first time. The results will be useful for further isolation and characterization studies.

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Venomics of the milos viper (Macrovipera schweizeri) unveils patterns of venom composition and exochemistry across blunt-nosed viper venoms

Schulte,

Damm,

Avella

et al. 2023

Front. Mol. Biosci.

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Introduction: Snakebite is a neglected tropical disease and a globally important driver of death and morbidity. Vipers of the genus Macrovipera (Viperidae: Viperinae) are among the snakes of higher medical importance in the Old World. Despite the medical relevance of Macrovipera venoms, the knowledge regarding them is heterogeneously distributed with virtually all works conducted so far focusing on subspecies of Macrovipera lebetinus, while other species within the genus are largely overlooked. Here we present the first proteomic evaluation of the venom from the Greek endemic Milos viper (Macrovipera schweizeri). In line with clinical symptoms typically elicited by Macrovipera envenomations, Milos viper venom primarily comprises coagulotoxic and cytotoxic protein families, such as metalloproteinases (svMP) and serine proteases (svSP).Methods: We conducted comparative bioactivity assays on venoms from M. schweizeri and the M. lebetinus subspecies M. lebetinus cernovi, M. lebetinus obtusa, and M. lebetinus turanica, and showed that they all exhibit similarities in levels of cytotoxicity proteolytic activity, and inhibition of prokaryotic growth. Lastly, we compared Macrovipera venom profiles by 1D-SDS-PAGE and RP-HPLC, as well as our proteomic data with previously published Macrovipera venom proteomes.Results and discussion: The analyzes performed to reveal that a general venom profile seems to be conserved across blunt-nosed vipers, and that, M. schweizeri envenomations, similarly to those caused by other blunt-nosed vipers, are able to cause significant tissue damage. The present work represents an important starting point for the development of comparative studies across the full taxonomic range of the genus Macrovipera and can potentially help optimize the treatment of envenomations caused by M. schweizeri.

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Cytotoxic Activities of the Crude Venoms of Macrovipera lebetina lebetina from Cyprus and M. l. obtusa from Turkey (Serpentes: Viperidae) on Human Umbilical Vein Endothelial Cells

Cited by 4 publications

References 22 publications

A Fourier Transform Infrared Spectroscopic Investigation of Macrovipera lebetina lebetina and M. l. obtusa Crude Venoms

A Fourier Transform Infrared Spectroscopic Investigation of Macrovipera lebetina lebetina and M. l. obtusa Crude Venoms

Determination of the fibrinogenolytic activity of Montivipera raddei (Raddeʼs mountain viper) venom

Venomics of the milos viper (Macrovipera schweizeri) unveils patterns of venom composition and exochemistry across blunt-nosed viper venoms

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