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Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata.

ABSTRACT: Amino acid sequences of three phospholipases A, I, III and IV, from the venom of the sea snake Laticauda semifasciata were elucidated. Each protein consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. They showed high homology among themselves, and with the other snake-venom phospholipases A and with the enzymes from mammalian pancreas. Phospholipases A III and IV were especially similar to each other, with only four differences out of their 118 amino acid residues. Phospholipase A I contained one tryptophan residue at position 64, which was important for enzymic activity, whereas III and IV did not contain tryptophan residues and their corresponding positions were occupied by leucine residues. The substitution by leucine resulted in a decreased, but definite, phospholipase A activity. The substituted enzymes have a more potent neuromuscular blocking activity. Full experimental details and evidence for the amino acid sequences of the proteins have been deposited as Supplementary Publication SUP 50118 (39 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem.J. (1981) 193, 5.

SUBMITTER: Nishida S

PROVIDER: S-EPMC1153902 | biostudies-other | 1982 Dec

REPOSITORIES: biostudies-other

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The amino acid sequences of erabutoxins, neurotoxic proteins of sea-snake (Laticauda semifasciata) venom.

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| S-EPMC1176801 | biostudies-other

The primary structure of the toxin Laticauda semifasciata III, a weak and reversibly acting neurotoxin from the venom of a sea snake, Laticauda semifasciata.

Project description:A weak and reversibly acting neurotoxic protein of Laticauda semifasciata venom, Laticauda semifasciata III (component LsIII), was sequenced. Component LsIII consists of 66 amino acid residues and has five disulphide bridges, one of which was located between residues 26 and 30. The weak and reversible neurotoxicity of component LsIII is discussed in relation to its structure, which falls between those of the neuro- and cardiotoxins of sea snakes and Elapidae snakes isolated and sequenced so far.

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Correction of the amino acid sequences of erabutoxins from the venom of the sea snake Laticauda semifasciata.

Project description:The amino acid sequences of erabutoxins a and b were reinvestigated. The previously reported sequences of Gln-His at positions 6 and 7, and of Pro-Ser at positions 18 and 19 of erabutoxins a and b were corrected to His-Gln and Ser-Pro respectively.

| S-EPMC1144790 | biostudies-other

Studies on sea-snake venoms. Crystallization of erabutoxins a and b from Laticauda semifasciata venom.

Project description:1. The toxic principles in the venom of the sea-snake Laticauda semifasciata were separated into two components by CM-cellulose chromatography and obtained in crystalline forms. They were named ;erabutoxins a and b'. 2. The homogeneity of each toxin was shown by rechromatography, by disk electrophoresis, by ultracentrifuging, by toxicity measurements before and after repeated crystallizations and by N-terminal analysis. 3. They had molecular weights of about 7000. Both of them contained 61 (or 62) amino acid residues/molecule. The only difference between erabutoxins a and b was that one of the aspartic acid (or asparagine) residues in erabutoxin a was replaced by a histidine residue in erabutoxin b. 4. Both of the toxins had LD(50) values of 0.15mug./g. body wt. for mice and 0.07mug./g. for rats. It was shown with frog-muscle preparations that they acted on postsynaptic membrane to block neuromuscular transmission.

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The disulphide bonds of erabutoxin a, a neurotoxic protein of a sea-snake (Laticauda semifasciata) venom.

Project description:Erabutoxin a was partially hydrolysed with enzymes and sulphuric acid and the resulting peptides were separated from each other by column chromatography and paper electrophoresis. From the results of amino acid analyses of the sulphur-containing peptides and their oxidized components, all four disulphide bridges in the toxin molecule were located. The disulphide bonds were found between half-cystine residues at positions 3 and 24, 17 and 41, 43 and 54, and 55 and 60 from the N-terminus.

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Northward dispersal of sea kraits (Laticauda semifasciata) beyond their typical range.

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| S-EPMC5482473 | biostudies-literature

The isolation of an easily reversible post-synaptic toxin from the venom of a sea snake, Laticauda semifasciata.

Project description:A weakly neurotoxic component (Ls-III) was isolated by CM-cellulose column chromatography from the venom of a sea snake Laticauda semifasciata. The content of component LsIII was about 10-20% of the venom as determined by u.v. absorption at 280nm. Component LsIII was homogeneous on rechromatography and disc electrophoresis, and its molecular weight was shown to be 7100 by ultracentrifugation and 7300 by sodium dodecyl sulphate-polyacrylamide-gel disc electrophoresis. The isoelectric point of component LsIII was pH7.2. Component LsIII consisted of 66 amino acid residues including 10 half-cystine residues. The LD(50) of component LsIII by intramuscular injection was 1.24mug/g body wt. for mice and 0.45mug/g for baby chicks, which is about eight to ten times less toxic than erabutoxins a, b and c, all of which are contained in the same venom. Experiments with three isolated muscle preparations from different species indicated that component LsIII was a post-synaptically acting toxin, the action of which was easily reversed by washing.

| S-EPMC1168090 | biostudies-other

The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B.

Project description:Snake venom phospholipases B (SVPLBs) are the least studied enzymes. They constitute about 1% of Bothrops crude venoms, however, in other snake venoms, it is present in less than 1%. These enzymes are considered the most potent hemolytic agent in the venom. Currently, no structural information is available about these enzymes from snake venom. To better understand its three-dimensional structure and mechanisms of envenomation, the current work describes the first model-based structure report of this enzyme from Bothrops moojeni venom named as B. moojeni phospholipase B (PLB_Bm). The structure model of PLB_Bm was generated using model building software like I-TESSER, MODELLER 9v19, and Swiss-Model. The build PLB_Bm model was validated using validation tools (PROCHECK, ERRAT, and Verif3D). The analysis of the PLB_Bm modeled structure indicates that it contains 491 amino acid residues that form a well-defined four-layer αββα sandwich core and has a typical fold of the N-terminal nucleophile aminohydrolase (Ntn-hydrolase). The overall structure of PLB_Bm contains 18 β-strands and 17 α-helices with many connecting loops. The structure divides into two chains (A and B) after maturation. The A chain is smaller and contains 207 amino acid residues, whereas the B chain is larger and contains 266 amino acid residues. The sequence and structural comparison among homologous snake venom, bacterial, and mammals PLBs indicate that differences in the length and sequence composition may confer variable substrate specificity to these enzymes. Moreover, the surface charge distribution, average volume, and depth of the active site cavity also vary in these enzymes. The present work will provide more information about the structure-function relationship and mechanism of action of these enzymes in snakebite envenomation.

| S-EPMC7419708 | biostudies-literature

Amino acid sequences of two novel long-chain neurotoxins from the venom of the sea snake Laticauda colubrina.

Project description:From the venom of a population of the sea snake Laticauda colubrina from the Solomon Islands, a neurotoxic component, Laticauda colubrina a (toxin Lc a), was isolated in 16.6% (A280) yield. Similarly, from the venom of a population of L. colubrina from the Philippines, a neurotoxic component, Laticauda colubrina b (toxin Lc b), was obtained in 10.0% (A280) yield. The LD50 values of these toxins were 0.12 microgram/g body wt. on intramuscular injection in mice. Toxins Lc a and Lc b were each composed of molecules containing 69 amino acid residues with eight half-cystine residues. The complete amino acid sequences of these two toxins were elucidated. Toxins Lc a and Lc b are different from each other at five positions of their sequences, namely at positions 31 (Phe/Ser), 32 (Leu/Ile), 33 (Lys/Arg), 50 (Pro/Arg) and 53 (Asp/His) (residues in parentheses give the residues in toxins Lc a and Lc b respectively). Toxins Lc a and Lc b have a novel structure in that they have only four disulphide bridges, although the whole amino acid sequences are homologous to those of other known long-chain neurotoxins. It is remarkable that toxins Lc a and Lc b are not coexistent at the detection error of 6% of the other toxin. Populations of Laticauda colubrina from the Solomon Islands and from the Philippines have either toxin Lc a or toxin Lc b and not both of them.

| S-EPMC1153851 | biostudies-other

Short Linear Motifs Characterizing Snake Venom and Mammalian Phospholipases A2.

Project description:Snake venom phospholipases A2 (PLA2s) have sequences and structures very similar to those of mammalian group I and II secretory PLA2s, but they possess many toxic properties, ranging from the inhibition of coagulation to the blockage of nerve transmission, and the induction of muscle necrosis. The biological properties of these proteins are not only due to their enzymatic activity, but also to protein-protein interactions which are still unidentified. Here, we compare sequence alignments of snake venom and mammalian PLA2s, grouped according to their structure and biological activity, looking for differences that can justify their different behavior. This bioinformatics analysis has evidenced three distinct regions, two central and one C-terminal, having amino acid compositions that distinguish the different categories of PLA2s. In these regions, we identified short linear motifs (SLiMs), peptide modules involved in protein-protein interactions, conserved in mammalian and not in snake venom PLA2s, or vice versa. The different content in the SLiMs of snake venom with respect to mammalian PLA2s may result in the formation of protein membrane complexes having a toxic activity, or in the formation of complexes whose activity cannot be blocked due to the lack of switches in the toxic PLA2s, as the motif recognized by the prolyl isomerase Pin1.

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