Prediction of Antigenic Sites in Follicle-Stimulating Hormones: Difference Profiles Enhance Antigenicity Prediction Methods*

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Abstract
A method of predicting antigenic sites in proteins using only the information provided by primary structure has been reported. The basis of this method is that hydrophilic regions of a polypeptide should contain antigenic sites, since hydrophobic sites should be buried and inaccessible. However, if the antigen is homologous with a naturally occurring polypeptide in the immunized animal, the immune system may not recognize the predicted antigenic site as non-self. Therefore, a modification of the prediction scheme has been developed which can simultaneously examine a protein and its homolog. This method would predict as epitopes those sites that are hydrophilic (accessible) and unrelated to the host homolog (non-self). A computer program has been developed to compare polypeptides and generate difference profiles for antigenic sites. The method has been used to distinguish the antigenic determinants of ovine and human FSH.