Previous evidence had indicated that selected antigens contained in H. polygyrus adult worm homogenate (AWH) could bind non-specifically to mouse IgG1. To determine whether H. polygyrus superantigen was one of these binding molecules, an inhibition assay was carried out using monoclonal antibodies (MoAb) to block the in vitro superantigen response. The results indicated that non-specific IgG1 binding could inhibit the cellular response to the superantigen. This assumption was tested using affinity chromatography to extract those antigens which bound non-specifically to mouse IgG1. Both the protein fraction which bound to the column and the unfractionated AWH demonstrated superantigen activity, as described previously. In contrast, the unbound fraction contained no superantigen activity. None of the tested fractions exhibited non-specific mitogen activity. These results indicate that the superantigen produced by H. polygyrus binds to host IgG1 of any specificity and this binding can inhibit further host recognition of this molecule. Additionally, it was demonstrated that an apparently similar superantigen is also contained in L4 homogenate, and is strongly represented in the excretory/secretory (E/S) proteins produced by both adult and L4 parasitic states. Therefore, it is probably that H. polygyrus superantigen influences the host during both the L4 and adult stages of the life-cycle.
|Original language||English (US)|
|Number of pages||6|
|State||Published - 1997|
- Heligmosomoides polygyrus
ASJC Scopus subject areas