scholarly journals Comprehensive snake venomics of the Okinawa Habu pit viper, Protobothrops flavoviridis, by complementary mass spectrometry-guided approaches

2018 ◽  
Author(s):  
Maik Damm ◽  
Benjamin-Florian Hempel ◽  
Ayse Nalbantsoy ◽  
Roderich D. Süssmuth
Keyword(s):  
Mass Spectrometry ◽  
Snake Venom ◽  
Proteomic Analysis ◽  
Top Down ◽  
Crude Venom ◽  
Human Neuroblastoma ◽  
Phospholipases A2 ◽  
Cytotoxicity Assays ◽  
Intact Mass ◽  
Snake Venomics

The Asian world is home to a multitude of venomous and dangerous snakes, which are attributed to various medical effects used in the preparation of traditional snake tinctures and alcoholics, like the Japanese snake wine, named Habushu. The aim of this work was to perform the first quantitative proteomic analysis of the Protobothrops flavoviridis pit viper venom. Accordingly, the venom was analyzed by complimentary bottom-up and top-down mass spectrometry techniques. The mass spectrometry-based snake venomics approach revealed that more than half of the venom is composed of different phospholipases A2 (PLA2). The combination with an intact mass profiling led to the identification of the three main Habu PLA2s. Furthermore, nearly one-third of the total venom consists of snake venom metalloproteinases and disintegrins, and several minor represented toxins families were detected: CTL, CRISP, svSP, LAAO, PDE and 5’-nucleotidase. Finally, the venom of P. flavoviridis contains certain bradykinin-potentiating peptides and related peptides, like the svMP inhibitors pEKW, pEQW, pEEW and pENW. In preliminary MTT cytotoxicity assays the highest cancerous-cytotoxicity of the crude venom was measured against human neuroblastoma SH-SY5Y cells and shows in some fractions disintegrin-like effects.

scholarly journals Comprehensive Snake Venomics of the Okinawa Habu Pit Viper, Protobothrops flavoviridis, by Complementary Mass Spectrometry-Guided Approaches

Molecules ◽  
2018 ◽  
Vol 23 (8) ◽  
pp. 1893 ◽  
Author(s):  
Maik Damm ◽  
Benjamin-Florian Hempel ◽  
Ayse Nalbantsoy ◽  
Roderich Süssmuth
Keyword(s):  
Mass Spectrometry ◽  
Snake Venom ◽  
Serine Proteases ◽  
Secretory Proteins ◽  
Crude Venom ◽  
Human Neuroblastoma ◽  
Phospholipases A2 ◽  
Cytotoxicity Assays ◽  
Intact Mass ◽  
Snake Venomics

The Asian world is home to a multitude of venomous and dangerous snakes, which are used to induce various medical effects in the preparation of traditional snake tinctures and alcoholics, like the Japanese snake wine, named Habushu. The aim of this work was to perform the first quantitative proteomic analysis of the Protobothrops flavoviridis pit viper venom. Accordingly, the venom was analyzed by complimentary bottom-up and top-down mass spectrometry techniques. The mass spectrometry-based snake venomics approach revealed that more than half of the venom is composed of different phospholipases A2 (PLA2). The combination of this approach and an intact mass profiling led to the identification of the three main Habu PLA2s. Furthermore, nearly one-third of the total venom consists of snake venom metalloproteinases and disintegrins, and several minor represented toxin families were detected: C-type lectin-like proteins (CTL), cysteine-rich secretory proteins (CRISP), snake venom serine proteases (svSP), l-amino acid oxidases (LAAO), phosphodiesterase (PDE) and 5′-nucleotidase. Finally, the venom of P. flavoviridis contains certain bradykinin-potentiating peptides and related peptides, like the svMP inhibitors, pEKW, pEQW, pEEW and pENW. In preliminary MTT cytotoxicity assays, the highest cancerous-cytotoxicity of crude venom was measured against human neuroblastoma SH-SY5Y cells and shows disintegrin-like effects in some fractions.

scholarly journals Mass spectrometry‐based top‐down and bottom‐up approaches for proteomic analysis of the Moroccan Buthus occitanus scorpion venom

FEBS Open Bio ◽  
2021 ◽  
Author(s):  
Khadija Daoudi ◽  
Christian Malosse ◽  
Ayoub Lafnoune ◽  
Bouchra Darkaoui ◽  
Salma Chakir ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Scorpion Venom ◽  
Top Down ◽  
Bottom Up

scholarly journals Top-down and middle-down proteomic analysis of Shiga toxin using MALDI-TOF-TOF mass spectrometry

MethodsX ◽  
2019 ◽  
Vol 6 ◽  
pp. 815-826 ◽  
Author(s):  
Clifton K. Fagerquist ◽  
William J. Zaragoza
Keyword(s):  
Mass Spectrometry ◽  
Shiga Toxin ◽  
Proteomic Analysis ◽  
Top Down ◽  
Maldi Tof

scholarly journals In-depth proteomic analysis of human tropomyosin by top-down mass spectrometry

2013 ◽  
Vol 34 (3-4) ◽  
pp. 199-210 ◽  
Author(s):  
Ying Peng ◽  
Deyang Yu ◽  
Zachery Gregorich ◽  
Xin Chen ◽  
Andreas M. Beyer ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Top Down ◽  
Top Down Mass Spectrometry

scholarly journals Snake venomics of Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia

2013 ◽  
Author(s):  
Maritza Fernández Culma ◽  
Jaime A Pereañez ◽  
Vitelbina Núñez Rangel ◽  
Bruno Lomonte
Keyword(s):  
Amino Acid ◽  
Protein Composition ◽  
Secretory Proteins ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Analytical Strategy ◽  
Phospholipases A2 ◽  
Snake Venomics

Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panamá, Colombia, and Ecuador, whose venom is poorly characterized. In the present work, the protein composition of this venom was profiled using the 'snake venomics' analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.

scholarly journals Transcriptomic and Proteomic Analysis of the Tentacles and Mucus of Anthopleura dowii Verrill, 1869

Marine Drugs ◽  
2019 ◽  
Vol 17 (8) ◽  
pp. 436 ◽  
Author(s):  
Santos Ramírez-Carreto ◽  
Rosario Vera-Estrella ◽  
Tobías Portillo-Bobadilla ◽  
Alexei Licea-Navarro ◽  
Johanna Bernaldez-Sarabia ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Sea Anemone ◽  
Global Perspective ◽  
Tandem Mass ◽  
Proteomic Profile ◽  
Na Channels ◽  
Sea Anemones ◽  
Phospholipases A2 ◽  
Proteomic Data

Sea anemone venom contains a complex and diverse arsenal of peptides and proteins of pharmacological and biotechnological interest, however, only venom from a few species has been explored from a global perspective to date. In the present study, we identified the polypeptides present in the venom of the sea anemone Anthopleura dowii Verrill, 1869 through a transcriptomic and proteomic analysis of the tentacles and the proteomic profile of the secreted mucus. In our transcriptomic results, we identified 261 polypeptides related to or predicted to be secreted in the venom, including proteases, neurotoxins that could act as either potassium (K+) or sodium (Na+) channels inhibitors, protease inhibitors, phospholipases A2, and other polypeptides. Our proteomic data allowed the identification of 156 polypeptides—48 exclusively identified in the mucus, 20 in the tentacles, and 88 in both protein samples. Only 23 polypeptides identified by tandem mass spectrometry (MS/MS) were related to the venom and 21 exclusively identified in the mucus, most corresponding to neurotoxins and hydrolases. Our data contribute to the knowledge of evolutionary and venomic analyses of cnidarians, particularly of sea anemones.

scholarly journals Snake venomics of Bothrops punctatus, a semi-arboreal pitviper species from Antioquia, Colombia

2013 ◽  
Author(s):  
Maritza Fernández Culma ◽  
Jaime A Pereañez ◽  
Vitelbina Núñez Rangel ◽  
Bruno Lomonte
Keyword(s):  
Amino Acid ◽  
Protein Composition ◽  
Secretory Proteins ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Analytical Strategy ◽  
Phospholipases A2 ◽  
Snake Venomics

Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panamá, Colombia, and Ecuador, whose venom is poorly characterized. In the present work, the protein composition of this venom was profiled using the 'snake venomics' analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (9.3%), serine proteinases (5.4%), disintegrins (3.8%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (1.7%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.

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