Abstract
Objective: The spike (S) protein of porcine hemagglutinating encephalomyelitis virus (PHEV) may mediate infection by binding to a cellular neural cell adhesion molecule (NCAM). This study aimed to identify the crucial domain of the S1 subunit of the S protein that interacts with NCAM. Methods: Three truncated segments (S<sub>1-291</sub>, S<sub>277-794</sub> and S<sub>548-868</sub>) of the S gene of PHEV and the NCAM gene were cloned individually into the Escherichia coli expression vectors and yeast two-hybrid expression vectors. The interaction between S<sub>1-291</sub>, S<sub>277-794</sub>, S<sub>548-868</sub> and NCAM were detected by a GST pull-down experiment and yeast two-hybrid assay. Results: Three fusion proteins (S<sub>1-291</sub>, S<sub>277-794</sub> and S<sub>548-868</sub>) were screened for their interactions with NCAM by protein-protein interaction assays. The results of these assays clarified that S<sub>277-794</sub> interacted with NCAM, while S<sub>1-291</sub> and S<sub>548-868</sub> did not. Conclusions: A small fragment (258-amino-acid fragment, residues 291-548) on the PHEV S protein was posited to be the minimum number of amino acids necessary to interact with NCAM. This fragment may be the receptor-binding domain that mediates PHEV binding to NCAM.
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