@article{f3fdefbc4e5d4b5fb0964fd058d0d8f8,
title = "Identification of proteins from venom of the paralytic spider wasp, Cyphononyx dorsalis",
abstract = "The solitary spider wasp Cyphononyx dorsalis is well known to hunt spiders: it uses its stinger to paralyze its prey to feed its larva. This wasp venom was fractionated by bioassay-guided chromatography. Cation-exchange chromatography indicated that the pI value of the active principle was >6.5. 2D-PAGE analysis of the active fraction obtained by gel permeation chromatography showed three major spots of proteins. Two that appeared at pI of >6.5 were analyzed by in-gel digestion and protein sequencing. Three proteins were identified: an arginine kinase-like protein that was highly homologous to that of honeybee, an elastase like-protein that was homologous to that of fire ant, and an unknown protein that was not homologous to any protein in the database. Recombinant proteins expressed in E. coli were purified and used for bioassay. The results showed that the arginine kinase-like protein exhibited paralytic activity against spiders with the same characteristic symptoms as the crude venom.",
keywords = "Arginine kinase, Cyphononyx dorsalis, Elastase, Paralysis, Pompilidae, Venom, Wasp",
author = "Tsuyoshi Yamamoto and Hirokazu Arimoto and Tomoya Kinumi and Yuichi Oba and Daisuke Uemura",
note = "Funding Information: We thank Dr. Yasuaki Okumura (Shizuoka University) for his invaluable suggestions, Dr. Tomoji Endo (Kobe College) for identifying wasps, Dr. Michiyasu Yoshikuni (National Institute for Basic Biology, Aichi, Japan) for his help with the purification and analysis of proteins, Drs. Tomohiko Suzuki and Kouji Uda (Kochi University) for the generous gift of arginine kinase and their helpful discussions, Mr. Akihiko Yawata for supplying spiders, and Drs. Masahiro Uritani and Hideo Dohra and Ms. Hiroko Sato (Shizuoka University) for their helpful discussions, and the reviewer of this manuscript for the suggesting a possible role of truncated arginine kinase-like protein. The amino acid sequence analysis was performed, in part, at The Center for Analytical Instruments, National Institute for Basic Biology (Aichi, Japan). This work was supported, in part, by Grants-in Aid for Scientific Research on Priority Areas (12045235 for D.U., 12045231 for H.A.), Creative Scientific Research (16GS0206), Exploratory Research (15651093 for H.A.), and the 21st century COE program (Establishment of COE on Materials Science) from MEXT, Japan. H.A. is also indebted to PRESTO, JST for support.",
year = "2007",
month = mar,
doi = "10.1016/j.ibmb.2006.12.001",
language = "English",
volume = "37",
pages = "278--286",
journal = "Insect Biochemistry and Molecular Biology",
issn = "0965-1748",
publisher = "Elsevier Limited",
number = "3",
}