Novel Biologically Active Peptides from the Venom of Polistes rothneyi iwatai

• Published in: Biological & Pharmaceutical Bulletin Vol. 29; no. 12; pp. 2493 - 2497
• Main Authors: Murata, Kazuya, Shinada, Tetsuro, Ohfune, Yasufumi, Hisada, Miki, Yasuda, Akikazu, Naoki, Hideo, Nakajima, Terumi
• Format: Journal Article
• Language: English
• Published: Japan The Pharmaceutical Society of Japan 01.12.2006; Pharmaceutical Society of Japan; Japan Science and Technology Agency
• Subjects: Amino Acid Sequence; Animals; Cells, Cultured; Chromatography, High Pressure Liquid; Female; heamolytic acitivity; Histamine Release - drug effects; histamine-releasing activity; Molecular Sequence Data; Peptides - isolation & purification; Peptides - pharmacology; polistes-mastoparan; polistes-protonectin; Rats; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; venom; wasp; Wasp Venoms - chemistry
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.29.2493

Four novel peptides, polistes-mastoparan-R1, 2, 3, and polistes-protonectin, were isolated from the venom of a paper wasp, Polistes rothneyi iwatai. MALDI-TOF MS analysis of a small amount of the crude venom gave six molecular-related ion peaks. Among them, m/z 1565 was expected to be a novel peptide. Purification of the crude venom by HPLC gave two known kinins, Thr6-bradykinin and Ala-Arg-Thr6-bradykinin, and four novel peptides named polistes-mastoparan-R1, 2, and 3, and polistes-protonectin. Polistes-mastoparan-R1, 2, and 3 (Pm-R) were tetradecapeptides that possess high sequence homology with that of mastoparan. The sequence of polistes-protonectin was similar to that of protonectin isolated from a Brazilian paper wasp. Histamine-releasing activities of Pm-R1, 2, and 3 were more potent than that of mastoparan. Polistes-protonectin exhibited the most potent hemolytic activity in comparison with the four novel peptides and mastoparan.