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

2013 ◽  
Vol 455 (2) ◽  
pp. 239-250 ◽  
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.

Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong
Keyword(s):  
Snake Venom ◽  
Protein Families ◽  
Traditional Medicines ◽  
Phospholipases A2 ◽  
Inhibitory Peptides ◽  
Sds Page ◽  
Deinagkistrodon Acutus ◽  
Venom Proteins ◽  
Proteins And Peptides

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.

One-pot hydrazide-based native chemical ligation for efficient chemical synthesis and structure determination of toxin Mambalgin-1

2014 ◽  
Vol 50 (44) ◽  
pp. 5837-5839 ◽  
Author(s):  
Man Pan ◽  
Yao He ◽  
Ming Wen ◽  
Fangming Wu ◽  
Demeng Sun ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Snake Venom ◽  
Structure Determination ◽  
Native Chemical Ligation ◽  
One Pot ◽  
Chemical Ligation ◽  
Venom Toxin ◽  
Snake Venom Toxin ◽  
Switch Strategy

An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation.

scholarly journals The mechanism of Ca2+ releasing action of a snake venom toxin in sarcoplasmic reticulum

1992 ◽  
Vol 58 ◽  
pp. 208
Author(s):  
Kaori Funayama ◽  
Ken-Ichi Furukawa ◽  
Yoshiteru Ohshima ◽  
Anthony T. Tu ◽  
Yasushi Ohizumi
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Snake Venom ◽  
Venom Toxin ◽  
Snake Venom Toxin

P-788 The snake venom toxin taipoxin confers specific toxicity to smallcell lung cancer cell lines

Lung Cancer ◽  
2005 ◽  
Vol 49 ◽  
pp. S326-S327
Author(s):  
T. Poulsen ◽  
N. Pedersen ◽  
M. Pedersen ◽  
H. Poulsen
Keyword(s):  
Lung Cancer ◽  
Cell Lines ◽  
Cancer Cell ◽  
Snake Venom ◽  
Cancer Cell Lines ◽  
Lung Cancer Cell ◽  
Venom Toxin ◽  
Snake Venom Toxin

Purification, sequencing and characterization of single amino acid-substituted phospholipase A2 isozymes from Trimeresurus Gramineus (green habu snake) venom

Toxicon ◽  
1993 ◽  
Vol 31 (8) ◽  
pp. 957-967 ◽  
Author(s):  
Toyoka Fukagawa ◽  
Takeru Nose ◽  
Yasuyuki Shimohigashi ◽  
Tomohisa Ogawa ◽  
Naoko Oda ◽  
...  
Keyword(s):  
Amino Acid ◽  
Phospholipase A2 ◽  
Snake Venom ◽  
Single Amino Acid

Amino acid sequence of a snake venom toxin that binds to the muscarinic acetylcholine receptor

Toxicon ◽  
1991 ◽  
Vol 29 (4-5) ◽  
pp. 521-526 ◽  
Author(s):  
Evert Karlsson ◽  
Carl Risinger ◽  
Mikael Jolkkonen ◽  
Christer Wernstedt ◽  
Abdu Adem
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acetylcholine Receptor ◽  
Snake Venom ◽  
Muscarinic Acetylcholine Receptor ◽  
Muscarinic Acetylcholine ◽  
Venom Toxin ◽  
Snake Venom Toxin

Molecular characterization of an acidic phospholipase A2 from Bothrops pirajai snake venom: synthetic C-terminal peptide identifies its antiplatelet region

2011 ◽  
Vol 85 (10) ◽  
pp. 1219-1233 ◽  
Author(s):  
Sabrina S. Teixeira ◽  
Lucas B. Silveira ◽  
Franco M. N. da Silva ◽  
Daniela P. Marchi-Salvador ◽  
Floriano P. Silva ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Molecular Characterization ◽  
Snake Venom ◽  
Bothrops Pirajai

Similarity of endothelin to snake venom toxin

Nature ◽  
1988 ◽  
Vol 335 (6188) ◽  
pp. 303-303 ◽  
Author(s):  
CHIKAHISA TAKASAKI ◽  
MASASHI YANAGISAWA ◽  
SADAO KIMURA ◽  
KATSUTOSHI GOTO ◽  
TOMOH MASAKI
Keyword(s):  
Snake Venom ◽  
Venom Toxin ◽  
Snake Venom Toxin
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