Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A₂homologue fromZhaoermia mangshanensisvenom

Abstract

Zhaoermiatoxin, an Arg49 phospholipase A 2 homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA 2 -homologue family that possesses an arginine residue at position 49, probably arising from a secondary Lys49!Arg substitution that does not alter the catalytic inactivity towards phospholipids. Like other Lys49 PLA 2 homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA 2 catalytic activity. A single crystal with maximum dimensions of 0.2 Â 0.2 Â 0.5 mm was used for X-ray diffraction data collection to a resolution of 2.05 Å using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P6 4 , with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 Å .

Differential gene expression profiles in the venom gland/sac of Orancistrocerus drewseni (Hymenoptera: Eumenidae)

“…Amino acid substitutions in the active site or Ca 21 -binding loop have been also reported in Group I and II PLA2s (Valentin and Lambeau, 2000). Among them, several catalytically inactive PLA2s from snake, where the critical Asp49 residue is substituted with Lys, Ser, or Arg, have been demonstrated to retain Ca 21 -independent pharmacological and antibacterial activities (Murakami et al, 2007;Paramo et al, 1998;Petan et al, 2007;Ward et al, 1998). These studies reveal that biological activities of venom PLA2s are not simply correlated with their catalytic properties, suggesting that the PLA2 of O. drewseni could have the Ca 21 -independent venomous activity regardless of its lack of catalytic activity.…”