An antibody diagnostic for hymenopteran parasitism is specific for a homologue of elongation factor-1 alpha.

An enzyme-linked immunosorbent assay (ELISA) useful for identifying noctuid pests parasitized by hymenopteran endoparasitoids was recently described. The ELISA employed a monoclonal antibody (MAb 9A5) that appeared highly polyspecific for parasitoid antigens, yielding banding patterns more typical of a polyclonal antiserum than of a monoclonal antibody in immunoblots of parasitoid homogenates subjected to SDS-PAGE. Although MAb 9A5 appeared capable of binding to dozens of parasitoid antigens, no cross-reactivity for noctuid antigens was evident by either immunoblotting or ELISA. In the study described here, immunoprecipitation, SDS-PAGE, and N-terminus amino acid sequencing were used to identify the protein recognized by MAb 9A5 as a homologue of elongation factor-1 alpha (EF-1 alpha). The propensity for EF-1 alpha to bind to cytoskeletal components, the additional subunits of EF-1, and other proteins may account for the apparent polyspecificity of MAb 9A5 in immunoblots of whole-body parasitoid homogenates. The presence of a unique hymenopteran epitope suggests that EF-1 alpha molecules from other insect groups could similarly express novel determinants. These determinants may prove useful not only for insect detection, but also as targets for selective insecticides that act by inhibiting protein synthesis.