Antihuman growth hormone (GH) antibodies cross-react with the GH-like factor from plerocercoids of the tapeworm Spirometra mansonoides.

A factor produced by the plerocercoid stage of S. mansonoides mimics some, but not all, of the actions reported for hGH. The biological actions of plerocercoid growth factor (PGF) suggest structural similarity to human GH (hGH). Plerocercoid membranes were solubilized, and PGF was purified more than 1000-fold by hGH receptor affinity chromatography. The ability of purified PGF to displace [125I]hGH from monoclonal antibodies specific for four distinct nonoverlapping antigenic determinants of hGH and from an anti-hGH polyclonal antibody was tested in liquid phase RIA. All of the hGH antibodies cross-reacted with PGF, with potencies ranging from more than 60% to less than 1% that of the hGH standard. Of the four major epitopes of hGH defined by the monoclonal antibodies used in this study, only one is not represented to a significant extent in PGF. The epitope of hGH that is only marginally present in PGF is highly conformationally dependent, and a minor difference in the structure of PGF (compared to hGH) could result in a significant conformational change. The dramatic cross-reactivity between anti-hGH antibodies and PGF suggests that the similarities in biological activities between these two substances are based in significant molecular homology.