The affinities of monoclonal antibodies against core antigen of hepatitis B virus

Four monoclonal antibodies generated against the recombinant core antigen of hepatitis B virus are investigated for antigen binding. All exhibit a similar affinity to polystyrene-sorbed antigen but only one of them interacts with native form of HBcAg (an assembled particle) in solution. The presence of 0.1% sodium dodecylsulphate is required for the binding of other three antibodies. The phenomenon can be interpreted as inaccessibility of the corresponding epitopes unless the multimeric antigen structure is disrupted. The core antigen coated on polystyrene is considered as a similar exposed structure.