Zoanthids of the genus Palythoa are distributed worldwide in shallow waters around coral reefs. Like all cnidarians, they possess nematocysts that contain a large diversity of toxins that paralyze their prey. This work was aimed at isolating and functionally characterizing a cnidarian neurotoxic phospholipase named A2-PLTX-Pcb1a for the first time. This phospholipase was isolated from the venomous extract of the zoanthid Palythoa caribaeorum. This enzyme, which is Ca2+-dependent, is a 149 amino acid residue protein. The analysis of the A2-PLTX-Pcb1a sequence showed neurotoxic domain similitude with other neurotoxic sPLA2´s, but a different catalytic histidine domain. This is remarkable, since A2-PLTX-Pcb1a displays properties like those of other known PLA2 enzymes.
Anthozoa , Motor Cortex/drug effects , Neurotoxicity Syndromes , Neurotoxins/toxicity , Phospholipases A2/toxicity , Animals , Behavior, Animal/drug effects , Injections, Intraventricular , Male , Motor Activity/drug effects , Motor Cortex/pathology , Neurotoxins/chemistry , Neurotoxins/isolation & purification , Phospholipases A2/chemistry , Phospholipases A2/isolation & purification , Rats, Wistar
