Antimicrobial peptides from the venoms of Vespa bicolor Fabricius.
Hornets possess highly toxic venoms, which are rich in toxins, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms. Vespa mastoparan (MP-VBs) and Vespa chemotatic peptide presenting antimicrobial action (VESP-VBs) were purified and characterized from the venom of the wasp, Vespa bicolor Fabricius. The precursors encoding VESP-VBs and MP-VBs were cloned from the cDNA library of the venomous glands. Analyzed by FAB-MS, the amino acid sequence and molecular mass for VESP-VB1 were FMPIIGRLMSGSL and 1420.6, for MP-VB1 were INMKASAAVAKKLL and 1456.5, respectively. The primary structures of these peptides are homologous to those of chemotactic peptides and mastoparans isolated from other vespid venoms. These peptides showed strong antimicrobial activities against bacteria and fungi and induced mast cell degranulation, but displayed almost no hemolytic activity towards human blood red cells.
Chen
Wenhu
W
College of Life Sciences, Hebei Normal University, Shijiazhuang 050016, Hebei, China; Zhejiang Provincial Cancer Hospital, Hangzhou 310022, Zhejiang, China.
Yang
Xinbo
X
Yang
Xiaolong
X
Zhai
Lei
L
Lu
Zekuan
Z
Liu
Jingze
J
Yu
Haining
H
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000187:drug effects; D001483:Base Sequence; D003001:Cloning, Molecular; D005658:Fungi / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D011817:Rabbits; D014862:Wasp Venoms / Q000737:chemistry* / Q000494:pharmacology; D014863:Wasps / Q000737:chemistry*
D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D014862:Wasp Venoms; C037500:mastoparan