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Human noroviruses (HuNoVs) are the major viral pathogens of epidemic acute gastroenteritis. To develop an effective method for mining functional receptors of HuNoVs is the first step to know the interaction mechanism between HuNoVs and their hosts. A novel approach that incorporates the mining of viral receptors was introduced in this study by targeting the P domain of the major capsid protein from HuNoVs (GI.1 or GII.4) onto the surface of Escherichia colivia the N-terminal domain of the ice nucleation protein InaQ (InaQN). Results of growth curves demonstrated that the expression of fusion proteins did not influence the bacterial growth. After optimization of induction conditions, immunofluorescence microscopy was employed to confirm bacterial surface localization and antigenicity. Results revealed remarkable surface display ability and antigenicity properties. Therefore, bacterial surface displayed P domain can be a good candidate for further mining HuNoVs receptors in the environments.

Display of P Domain of Human Norovirus Major Capsid Protein on Escherichia Coli Surface