Isolation and Characterization of CvIV4: A Pain Inducing α- Scorpion Toxin
نویسندگان
چکیده
منابع مشابه
Isolation and Characterization of CvIV4: A Pain Inducing α- Scorpion Toxin
BACKGROUND Among scorpion species, the Buthidae produce the most deadly and painful venoms. However, little is known regarding the venom components that cause pain and their mechanism of action. Using a paw-licking assay (Mus musculus), this study compared the pain-inducing capabilities of venoms from two species of New World scorpion (Centruroides vittatus, C. exilicauda) belonging to the neur...
متن کاملA bimodal activation mechanism underlies scorpion toxin–induced pain
Venomous animals use peptide toxins for hunting and self-defense. To achieve these goals, toxins need to bind to their targets with high affinity due to the small amount that a single bite or sting can deliver. The scorpion toxin BmP01 is linked to sting-induced excruciating pain; however, the reported minimum concentrations for activating TRPV1 channel or inhibiting voltage-gated potassium (Kv...
متن کاملScorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel
The intense pain induced by scorpion sting is a frequent clinical manifestation. To date, there is no established protocol with significant efficacy to alleviate the pain induced by scorpion envenomation. One of the important reasons is that, little information on pain-inducing compound from scorpion venoms is available. Here, a pain-inducing peptide (BmP01) has been identified and characterize...
متن کاملCharacterization of cDNA sequence encoding for a novel sodium channel -toxin from the Iranian scorpion Mesobuthus eupeus venom glands
The venoms of Buthidae scorpions are known to contain basic, single-chain protein -toxins consisting of 60-70 amino acid residues that are tightly cross-linked by four disulfide bridges. Total RNA was extracted from the venom glands of scorpion Mesobuthus eupeus collected from the Khuzestan province of Iran and then cDNA was synthesized with the modified oligo (dT) primer and extracted total R...
متن کاملα-Scorpion Toxin Impairs a Conformational Change that Leads to Fast Inactivation of Muscle Sodium Channels
Alpha-scorpion toxins bind in a voltage-dependent way to site 3 of the sodium channels, which is partially formed by the loop connecting S3 and S4 segments of domain IV, slowing down fast inactivation. We have used Ts3, an alpha-scorpion toxin from the Brazilian scorpion Tityus serrulatus, to analyze the effects of this family of toxins on the muscle sodium channels expressed in Xenopus oocytes...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: PLoS ONE
سال: 2011
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0023520