Purification and characterization of raventoxin-I and raventoxin-III, two neurotoxic peptides from the venom of the spider Macrothele raveni.

نویسندگان

  • Xiong-Zhi Zeng
  • Qiao-Bin Xiao
  • Song-Ping Liang
چکیده

The spider Macrothele raveni was recently identified as a new species of Genus Macrothele. The crude venom from M. raveni was found to be neurotoxic to mice and the LD(50) of the crude venom in mice was 2.852mg/kg. Two neurotoxic peptides, raventoxin-I and raventoxin-III, were isolated from the crude venom by ion-exchange and reverse phase high performance liquid chromatography. Raventoxin-I was the most abundant toxic component in the venom, while raventoxin-III was a lower abundant component. Both toxins can kill mice and block neuromuscular transmission in an isolated mouse phrenic nerve diaphragm preparation, but have no effect on cockroaches. The LD(50) of raventoxin-I in mice is 0.772mg/kg. The complete amino acid sequences of raventoxin-I and raventoxin-III were determined and found to consist of 43 and 29 amino acid residues, respectively. It was determined by mass spectrometry that all Cys residues from raventoxin-I and raventoxin-III are involved in disulphide bonds. raventoxin-III showed no significant sequence homology with any presently known neurotoxins in the protein/DNA databases, while raventoxin-I has limited sequence identity with delta-AcTx-Hv1 and delta-AcTx-Ar1, which target both mammalian and insect sodium channels. Both raventoxin-I and raventoxin-III only work on vertebrates, but not on insects. Moreover, raventoxin-I could exert an effect of first exciting and then inhibiting the contraction of mouse diaphragm muscle caused by electrically stimulating the phrenic nerve, but raventoxin-III could not.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Purification and characterization of a novel type of neurotoxic peptides from the venom of the Iranian scorpion Hemiscorpius lepturus

Objective(s): Scorpion venom has toxic effects on mammals, insects and crustaceans.  Toxicogenic peptides are major contributors to the scorpion venom, which make it toxic. The Hemiscorpius lepturus (H. lepturus) is one of the most common scorpion bites agent, and responsible for 95% of scorpion bite deaths cases in Iran.Materials and Methods:</strong...

متن کامل

Identification and Purification of two Mammalian Nourotoxins from Iranian Scorpion (Buthotus schach) Venom

  Scorpion venoms contain of variety of peptides toxic to mammals ، insects and crustaceans. Toxic peptides are the main factors in scorpion venom causing toxicity, (their amount being 1-3%of total venom.). Most of the scorpion toxins have been isolated from the venoms of scorpions in the family Buthidae. The scorpion Buthotus Schach belonging to the Buthidae family is widely found in the weste...

متن کامل

Identification and Purification of BS413 Neurotoxin from Iranian Scorpion (Buthotus Schach) Venom

Introduction: Scorpion venoms contain a variety of peptides, toxic to mammals، insects and crustaceans and are the main factors in scorpion venom toxicity (their amount being 1-3% of total venom). Most of the scorpion toxins have been isolated from the venoms of scorpions in the Buthidae family. The scorpion Buthotus Schach of this family is widely found in the western regions of Iran, but no p...

متن کامل

A Novel Defensin-Like Peptide Associated with Two Other New Cationic Antimicrobial Peptides in Transcriptome of the Iranian Scorpion Venom

Introduction: Scorpion venom is a source of bioactive peptides, and some antimicrobial peptides (AMPs) have been found in the venom gland of scorpions. Therefore, the discovery of new anti-infective agents is an essential need to overcome the problem of antibiotic resistance of clinical isolates. Here, we describe three new cationic AMPs, including meuVAP-6, meuAP-18-1, and meuPep34 from the ve...

متن کامل

Partial Purification and Characterization of Anticoagulant Factor from the Snake (Echis carinatus) Venom

  Objective(s): Snake venoms contain complex mixture of proteins with biological activities. Some of these proteins affect blood coagulation and platelet function in different ways. Snake venom toxin may serve as a starting material for drug design to combat several pathophysiological problems such as cardiovascular disorders. In the present study, purification of anticoagulation facto...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Toxicon : official journal of the International Society on Toxinology

دوره 41 6  شماره 

صفحات  -

تاریخ انتشار 2003