Piscivorin
Encyclopedia
Piscivorin is a component of snake venom
secreted by the Eastern Cottonmouth
(Agkistrodon piscivorus piscivorus). It is a member of the cysteine-rich secretory protein
(CRISP) family, which blocks voltage-dependent calcium channels.
snake (Agkistrodon piscivorus piscivorus), which populates the Eastern United States. Typically, crude venom from the Eastern Cottonmouth contains approximately 1.25% of piscivorin.
The molecular mass of piscivorin is 24.842 kDa. The nucleotide sequence of piscivorin cDNA spans 1323 bp, containing an open reading frame of 240 codons.
Piscivorin has the following amino acid sequence.
-stimulated contraction of smooth muscle. Since caffeine normally causes contraction through the release of Ca2+ from the sarcoplasmic reticulum, this differential effect indicates that piscivorin is an L-type calcium channel
blocker. At a concentration of 1 μM, its effect on depolarization-induced smooth muscle contraction is weaker than of the related CRISP family toxins ablomin
, triflin
or latisemin
. A sequence comparison of piscivorin and other CRISP family proteins suggests that the Glu186 residue is the crucial site for the blocking of the calcium channels.
Unlike some other CRISP family proteins, piscivorin does not block cyclic nucleotide-gated channels.
Snake venom
Snake venom is highly modified saliva that is produced by special glands of certain species of snakes. The glands which secrete the zootoxin are a modification of the parotid salivary gland of other vertebrates, and are usually situated on each side of the head below and behind the eye,...
secreted by the Eastern Cottonmouth
Agkistrodon piscivorus
Agkistrodon piscivorus is a venomous snake, a species of pit viper, found in the southeastern United States. Adults are large and capable of delivering a painful and potentially fatal bite. When antagonized they will stand their ground by coiling their bodies and displaying their fangs...
(Agkistrodon piscivorus piscivorus). It is a member of the cysteine-rich secretory protein
Cysteine-rich secretory protein
Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins found exclusively in vertebrates. They are a subgroup of the CRISP, antigen 5 and Pr-1 protein superfamily and are substantially implicated in the functioning of the mammalian reproductive system...
(CRISP) family, which blocks voltage-dependent calcium channels.
Etymology
The name of piscivorin comes from the snake species name piscivorus, which is derived from the Latin words pisces and vorare, meaning 'fish' and 'to devour' respectively.Source
Piscivorin is produced in the venom glands of the Eastern CottonmouthAgkistrodon piscivorus
Agkistrodon piscivorus is a venomous snake, a species of pit viper, found in the southeastern United States. Adults are large and capable of delivering a painful and potentially fatal bite. When antagonized they will stand their ground by coiling their bodies and displaying their fangs...
snake (Agkistrodon piscivorus piscivorus), which populates the Eastern United States. Typically, crude venom from the Eastern Cottonmouth contains approximately 1.25% of piscivorin.
Biochemistry
Piscivorin belongs to the cysteine-rich secretory protein (CRISP) family, which are secreted as single-chain proteins with molecular masses between 20 and 30 kDa. They display significant amino acid sequence homology. Sixteen cysteine residues, forming 8 disulfide bonds, are strictly conserved in CRISPs. Ten of these cysteine residues are clustered into the C-terminal part of the protein.The molecular mass of piscivorin is 24.842 kDa. The nucleotide sequence of piscivorin cDNA spans 1323 bp, containing an open reading frame of 240 codons.
Piscivorin has the following amino acid sequence.
10 | 20 | 30 | 40 | 50 | 60 |
MIAFIVLPIL | AAVLQQSSGS | VDFDSESPRK | PEIQNQIVDL | HNSLRRSVNP | TASNMLKMEW |
70 | 80 | 90 | 100 | 110 | 120 |
YPEAAANAER | WAYRCIESHS | PRNSRVLGGI | KCGENIYMSS | IPIKWTEIIH | AWHGENKNFK |
130 | 140 | 150 | 160 | 170 | 180 |
YGIGADPPNA | VIGHFTQIVW | YKSYLVGCAA | AYCPSSEYSY | FYVCQYCPAG | NIIGKIATPY |
190 | 200 | 210 | 220 | 230 | 240 |
KSGPPCGDCP | SACVNGLCTN | PCTKEDKYTN | CKSLVQQYGC | QDKQMQSECS | AICFCQNKII |
Target and mode of action
Piscivorin reduces high potassium-evoked smooth muscle contraction, but does not inhibit caffeineCaffeine
Caffeine is a bitter, white crystalline xanthine alkaloid that acts as a stimulant drug. Caffeine is found in varying quantities in the seeds, leaves, and fruit of some plants, where it acts as a natural pesticide that paralyzes and kills certain insects feeding on the plants...
-stimulated contraction of smooth muscle. Since caffeine normally causes contraction through the release of Ca2+ from the sarcoplasmic reticulum, this differential effect indicates that piscivorin is an L-type calcium channel
L-type calcium channel
The L-type calcium channel is a type of voltage-dependent calcium channel. "L" stands for long-lasting referring to the length of activation. Like the others of this class, the α1 subunit is the one that determines most of the channel's properties....
blocker. At a concentration of 1 μM, its effect on depolarization-induced smooth muscle contraction is weaker than of the related CRISP family toxins ablomin
Ablomin
Ablomin is a toxin present in the venom of the Japanese Mamushi snake, which blocks L-type voltage-gated calcium channels.- Etymology :The protein ablomin is a component of the venom of the Japanese Mamushi snake, Gloydius blomhoffi...
, triflin
Triflin
Triflin is a cysteine-rich secretory protein , which is excreted by the venom gland of the Habu snake . Triflin reduces high potassium-induced smooth muscle contraction, suggesting a blocking effect on L-type calcium channels.- Source :Triflin is a toxin derived from snake venom...
or latisemin
Latisemin
Latisemin is a cysteine-rich secretory protein that can be isolated from the venom of the Black-banded sea krait, a sea snake indigineous to the warmer waters of the western Pacific Ocean...
. A sequence comparison of piscivorin and other CRISP family proteins suggests that the Glu186 residue is the crucial site for the blocking of the calcium channels.
Unlike some other CRISP family proteins, piscivorin does not block cyclic nucleotide-gated channels.