The first report of kininogen from invertebrates.
The hornet possesses highly toxic venom, which is rich in toxin, enzymes, and biologically active peptides. Several bradykinin-like peptides, vespakinins, have been found in wasp venoms since 1970s, but the mode of biosynthesis of these peptides is unknown. In the present study, a vespakinin M was purified from venom of Vespa magnifica. Its primary sequence was established as GRPPGFSPFRID. The cDNA encoding the vespakinin M was cloned from the cDNA library of V. magnifica venom gland. The cDNA structure of vespakinin M was found to contain a coding region of 168 nucleotides. The encoded precursor of vespakinin M is composed of a signal peptide, an acidic peptide, and a mature peptide of vespakinin M. This is the first kininogen from insects; it is also the first kininogen from invertebrates. The cDNA structure encoding vespakinin M suggests that the generation mode of bradykinin-related peptides in wasp is different from amphibian skin and mammalian blood system.
Zhou
Zuohong
Z
Key Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture, Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Yang
Hailong
H
Xu
Xueqing
X
Wang
Xu
X
Lai
Ren
R
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001920:Bradykinin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000302:isolation & purification; D007704:Kininogens / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D014862:Wasp Venoms / Q000737:chemistry; D014863:Wasps
D007704:Kininogens; D014862:Wasp Venoms; C014243:vespakinin-M; D001920:Bradykinin