Isolation and Structure of Pompilidotoxins, Novel Peptide Neurotoxins in Solitary Wasp Venoms

• Published in: Biochemical and biophysical research communications Vol. 250; no. 3; pp. 612 - 616
• Main Authors: Konno, Katsuhiro, Hisada, Miki, Itagaki, Yasuhiro, Naoki, Hideo, Kawai, Nobufumi, Miwa, Akiko, Yasuhara, Tadashi, Takayama, Hiroaki
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.09.1998
• Subjects: Animals; ANOPLIUS SAMARIENSIS; BACTOZONELLUS MACULIFRONS; Batozonellus maculifrons; Insect Proteins; INSOLACION; INSOLATION; Nephropidae; Neuromuscular Junction - drug effects; Neurotoxins - isolation & purification; Neurotoxins - pharmacology; Pompilidae; pompilidotoxin; Synaptic Transmission - drug effects; TOXINAS; TOXINE; TOXINS; VENENOS; VENIN; VENOMS; VESPIDAE; Wasp Venoms; Wasps
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1998.9299

Novel peptide neurotoxins, α- and β-pompilidotoxins (α- and β-PMTXs), were purified from the venoms of the solitary waspsAnoplius samariensisandBatozonellus maculifrons.Their structures were analyzed mostly by MALDI-TOF-MS, which were corroborated by solid-phase synthesis. α-PMTX, with 13 amino acid residues and the sequence of Arg-Ile-Lys-Ile-Gly-Leu-Phe-Gln-Asp-Leu-Ser-Lys-Leu-NH2, greatly potentiates synaptic transmission of lobster leg muscle by the presynaptic mechanisms. β-PMTX, in which the lysine residue at 12 position of α-PMTX was replaced with arginine, was more potent than α-PMTX.