Abstract
The structure and function of the C-terminus domain (CTD) of porcine transmissible gastroenteritis virus (TGEV) spike protein remain largely unknown, thereby a specific monoclonal antibody (MAb) allows us to fully understand this domain. In this study, we developed a murine MAb against CTD of TGEV spike protein, as evidenced by the results of indirect fluorescent assay, Western blotting, and fluorescence-activated cell sorter. Further study showed that the MAb is able to exclusively recognize a 12-residue peptide (FKNVSDGVIYSV) derived from CTD of TGEV spike protein. This MAb can be used to elucidate the potential function of CTD of TGEV spike in virus attachment and entry, and warrants further intensive investigation.
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