Identification of three novel peptides isolated from the venom of the neotropical social wasp Polistes major major.
Three novel peptides designated as PMM1, PMM2, and PMM3 were isolated and characterized from the venom of the social wasp Polistes major major, one of the most common wasps in the Dominican Republic. By Edman degradation, and MALDI-TOF and ESI-QTOF mass spectrometry, the primary sequences of these peptides were established as follows: PMM1, H-Lys-Arg-Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg-OH (1357.77 Da); PMM2, H-Ile-Asn-Trp-Lys-Lys-Ile-Ala-Ser-Ile-Gly-Lys-Glu-Val-Leu-Lys-Ala-Leu-NH2 (1909.19 Da); and PMM3, H-Phe-Leu-Ser-Ala-Leu-Leu-Gly-Met-Leu-Lys-Asn-Leu-NH2 (1317.78 Da). The suggested sequences were confirmed by MS analysis of peptide fragments obtained by enzymatic digestion. The peptide PMM1 is a lysyl-arginyl-Thr(6)-bradykinine that belongs to the wasp kinins group. The sequence of the PMM2 peptide is unique; it resembles somewhat the tetradecapeptide amides of the mastoparan group; however, the chain is extended by three additional amino acid residues. The sequence of PMM3 dodecapeptide is homologous to the peptides of the wasp chemotactic group.
Cerovský
Václav
V
Laboratory of Chemical Ecology, Stevens Institute of Technology, Punta Cana Center for Biodiversity and Sustainability, Punta Cana Resort & Club, Punta Cana, Dominican Republic. cerovsky@uochb.cas.cz
Pohl
Jan
J
Yang
Zhihua
Z
Alam
Naseer
N
Attygalle
Athula B
AB
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000032:analysis* / Q000302:isolation & purification*; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014862:Wasp Venoms / Q000737:chemistry*; D014863:Wasps / Q000737:chemistry*
D009842:Oligopeptides; D014862:Wasp Venoms