Mass spectrometric analysis of the immunodominant glycan epitope of Echinococcus granulosus antigen Ag5.

In previous work we showed that Ag5, a major diagnostic antigen from the metacestode of Echinococcus granulosus, possesses a dominant sugar epitope that upon removal results in abolition of most of the antigen immunoreactivity with patient sera. Analysis of this glycan modification has now been performed by western blotting and mass spectrometry. Reactivity to both a specific monoclonal antibody (TEPC15) and human C-reactive protein as well as the presence of a modification of 165 mass units, as detected by mass spectrometry of both glycopeptides and released N-glycans, indicated that the immunodominant sugar epitope of the Ag5 38kDa subunit is a biantennary structure modified by phosphorylcholine. We believe this is the first time that such a modification has been proven in cestodes and provides the structural basis for understanding the antigenicity of this major E. granulosus component.