PROTEOMIC ANALYSIS OF THE VENOM FROM THE ENDOPARASITOID WASP Pteromalus puparum (HYMENOPTERA: PTEROMALIDAE)

摘要

Parasitoid venom is a complex mixture of active substances with diversified biological functions. Because of its range of activities, venom is an important resource with respect to potential application in agriculture and medicine. Only a limited number of peptides, proteins, and enzymes have been identified and characterized from parasitoid venom. Here we describe a proteomic analysis of the venom from the endoparasitoid wasp Pteromalus puparum (Hymenoptera: Pteromalidae). Venom resolved by two-dimensional electrophoresis yielded 56 protein spots with major proteins in the pI range 4–7 and molecular mass range of 25–66.2 kDa. The amino acid sequences of the proteins were identified by mass spectrometry. Several venom proteins such as calreticulin, venom acid phosphatase, serine protease, arginine kinase, serine protease homolog, aminotransferase-like venom protein, and heat shock protein 70, were identified in silico based on their amino acid sequences. The full-length cDNAs of calreticulin andarginine kinase were cloned. Calreticulin showed 62% identity with calreticulin in the venom of Cotesia rubecula. Arginine kinase showed a high level of sequence identity (92%) with its counterpart in the venom of Cyphononyx dorsalis. RT-PCR analysis revealed that the transcript levels of calreticulin and arginine kinase were developmentally changed, suggesting a possible correlation with the oviposition process. This study contributes to our appreciation of a parasitoid wasp venom composition.