A Novel Phospholipase A2 Isolated from Palythoa caribaeorum Possesses Neurotoxic Activity

• Published in: Toxins Vol. 11; no. 2; p. 89
• Main Authors: Cuevas-Cruz, Miguel, Lazcano-Pérez, Fernando, Hernández-Guzmán, Ulises, Díaz de la Vega-Castañeda, Karen Helena, Román-González, Sergio A, Valdez-Cruz, Norma A, Velasco-Bejarano, Benjamín, Colín-González, Ana Laura, Santamaría, Abel, Gómez-Manzo, Saúl, Marcial-Quino, Jaime, Arreguín-Espinosa, Roberto
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.02.2019; MDPI
• Subjects: Amino acid sequence; Amino acids; Animals; Anthozoa; Behavior, Animal - drug effects; Binding sites; Calcium; Calcium ions; cnidaria; Coral reefs; Domains; Enzymes; Histidine; Injections, Intraventricular; Male; Motor Activity - drug effects; Motor Cortex - drug effects; Motor Cortex - pathology; Nematocysts; Neurotoxicity; Neurotoxicity Syndromes; neurotoxin; Neurotoxins - chemistry; Neurotoxins - isolation & purification; Neurotoxins - toxicity; Palythoa caribaeorum; Peptides; Phospholipase; Phospholipase A2; Phospholipases A2 - chemistry; Phospholipases A2 - isolation & purification; Phospholipases A2 - toxicity; Prey; Rats, Wistar; Shallow water; Toxins; Venom; neurotoxin; cnidaria; venom; Palythoa caribaeorum; phospholipase A2
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins11020089

Zoanthids of the genus 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 . This enzyme, which is Ca -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.