BIOCHEMICAL AND IMMUNOLOGICAL STUDIES OF PROTEINS FROM POLYDNAVIRUS CHELONUS SP-NEAR CURVIMACULATUS

Polydnavirus from Chelonus sp. curvimaculatus (CcV) was purified and 18 structural polypeptides associated with CcV were identified by silver staining. Antibodies were raised against CcV protein and used in testing for the presence of the virus in different tissues of the wasp ovary and in stung eggs. It was also established that the virus does not enter during the first 5 s of oviposition. Furthermore, no degradation of the virus proteins was detected inside the egg within 2 h after oviposition. The glycoprotein nature of virus proteins was also determined by concanavalin A/horseradish peroxidase staining. The amino acid compositions of the most highly abundant peptides (41K, 33K, 21K, 17K and 13K) were determined, as was the N-terminal amino acid sequence of the 41K protein. The latter did not show similarity with any reported protein sequences.